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Monthly Archives: December 2013

Bulk Peptides

Posted on December 30, 2013 by Maxim Peptide Posted in Peptide Research

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free shipping on bulk peptidesAs researchers improve the methods used to produce synthetic peptides, it is becoming easier to create larger batches of peptides at once. This is performed by creating chemical bonds that will mimic the reactions created by an animal’s body to produce a similar sequence of amino acids that would create a hormone or chemical reaction within the body. In some cases, the bonding sequence of the amino acids are altered when producing synthetic peptides because it can alter the reaction of the peptide or increase the half-life of the peptide once it is applied to an animal’s blood stream. Creating bulk peptides can pose difficulties for manufacturers as the process can be somewhat unpredictable. The proper methodology for creating bulk batches of peptides vary based on the nature of the chemical. The effectiveness of the methods used to create the necessary chemical bonds to create amino acid chains that produce peptides is still under review, and it is not uncommon for different companies to utilize different methods in order to create these chains. The key is utilizing methodologies that are determining the most appropriate method for creating bulk peptides is the process that ensures the highest level of consistency in the final batch of chemicals.

Reconstituting Bulk Peptide Batches

Every peptide will have different instructions, based on how it was formed and what chemicals are included in the bonds, but there are a few basic guidelines that should be followed to ensure that a viable solution is created.

  • If a peptide is designed to be used with a specific liquid, these instructions should be included with the powder. If the instructions do not make any particular specifications, bacteriostatic water can be used to re-constitute the powder. Almost all peptides can be safely combined with this substance; this is a very cost effective solution for researchers that are working with bulk sized batches.
  • There is an exception to this rule. IGF or any variations in this peptide should be reconstituted with acetic acid solutions. These typically cannot be combines with any other type of liquid.
  • The amount of liquid or peptide powder should be carefully measured before being inserted into a vial for application into a live animal test subject. Every peptide should contain a set amount of applications in the bottle, and this cannot be varied, due to the strength of the solution that was created. In general, the amount of peptide and research liquid that is added should always equal the same weight, which will be specified on the container. If there is no specification, be sure to contact your bulk peptide supplier to determine the proper instructions for this step. In most cases a bulk peptide order will also include syringes that are intended for use in animal testing in research facilities, to ensure accuracy with this part of the process.

The strength of an application can be altered as necessary by adding more or less of the peptide in a given solution, so long as the total weight of the solution remains the same within the syringe. This is a common method that is used to determine what application size is ideal to elicit the type of response that researchers are hoping to achieve. It is also helpful for determining what application sizes could be dangerous to inject into animal tissue because it elicits side-effects.

Creating Long Term Shipping Schedules

Companies that produce bulk sized amounts of peptides often create partnerships with research facilities— to continue providing the supplies necessary for long-term research projects.

  • Those that have a set schedule for ongoing trials can ensure that multiple shipments of peptides that coincide with this schedule.
  • Shipments of different types of peptides can be scheduled to better ensure that these materials can be compared in animal tissues. This is essential for any research that is working to determine what type of peptide is ideal for the type of reaction that is being triggered.

Bulk peptide suppliers can help researchers determine the best timing for receiving new shipments of product. Studies that will be ongoing for several years will need to work with multiple shipments of peptides to ensure that the peptides are fresh and stable enough to work effectively. Most peptides can be kept in cold storage for up to two years if they are kept sealed, moisture-free and only constituted when it comes time to apply them to animal test subjects. The necessary information to make these decisions should be available on the sale page for the given peptide, but a bulk peptide supplier can always be contacted to answer any additional questions.

Seeking out a Source for Bulk Peptides

The consistency of product that is made available from a company will help researchers determine whether or not it is appropriate to utilize these wares for their experiments.

  • Bulk peptide companies are often willing to share which methodologies they use to create peptides to researchers. This helps people increase the depth of their research by comparing the best methods for creating accurate or reliable peptides.
  • Bulk peptide producers will also typically share their accuracy rates for producing peptides. This will help researchers determine if these peptides are reliable enough to create reactions that can be used as a definitive benchmark for peptide reactions and the development of future research that will depend on the predictability of these reactions.
  • In addition to noting the purity level of a peptide that is listed with a sample available for purchase, it is important to note which method was used to determine this purity ranking. If this information is not available on a sales page, the company should be forthcoming with this information.
  • The only way to fully determine the purity of a sample is to perform a full amino acid analysis. While it is impossible to do this on a full bulk sample, there is a range of testing procedures— including mass spec, HPLC and SDS page— that can provide an indication of what is included in this sample. However, the more chemicals and mixtures included in a component, the less accurate methods such as HPLC will be in determining purity, which can influence the safety of using these samples in a research setting.

A great deal of consideration must be given to the storage of peptides after they have been purchased. They must be kept in containers that will ensure that other particles, particularly moisture inducing elements are not able to interact with the peptide. This will damage the structures of the amino acids and can cause a breakdown in their chemical structure. Similarly, it is also essential that peptides are kept at a consistent temperature to avoid damage during transit and before they are applied to animal tissues. Once a peptide is received by a research facility similar care must be given to ensure that peptides are not damaged or begin breaking down before they have been applied to the animal tissues. Instructions for how peptides should be reconstituted and applied should be included with the vials so that a consistent procedure can be followed during this phase of an experiment. Typically, peptides should only be reconstituted when they are to be applied to the animal test subject, though some are able to remain in their constituted form for up to two weeks without the fear that they will begin showing signs of instability.

Resource Box:

http://en.wikipedia.org/wiki/Peptide_sequence

Buy The Best Peptides

Posted on December 27, 2013 by Maxim Peptide Posted in Peptide Research

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buy the best peptidesPeptides are gaining a great deal of attention in the scientific market today. These chemicals are naturally developed from amino acids in the body and can be used both as triggers and messengers– to create certain reactions within groups of tissue. Peptides can cause seemingly endless reactions within the body, depending on how they are triggered and which tissues they interact with.

It is believed that if peptides can be produced synthetically, they could have a strong pharmaceutical use. Testing on animals, tissue samples and other means are currently being worked by the scientist— to determine how these peptides could be used in pharmaceutical applications in the future.

Naturally, peptides have a very short time period where they are viable for use by bodily tissues. They are designed to break down quickly once they enter the bloodstream so that an animal’s body can harvest the various amino acids that make up these chains and use them for a variety of reactions as necessary.

This limits the ability to harvest these peptides and apply them in a research setting because long peptides that break down very quickly cannot be stored or given any type of shelf life. A variety of alterations to the build of common peptides have been suggested, as a means of addressing this issue.

Storing and Using Peptides in Research

Even the best peptides still have limitations that should be considered when purchasing large quantities of chemicals in a research project.

  • Proper storage and transport of a peptide is essential to maintaining its composition. Top peptide suppliers typically ship peptides in lyophilized form— with the intention of having them stored in hydroscopic form, to maintain the structure of the chemical for as long as possible. To further ensure the quality of the peptides, a desiccator should be used to ensure that they are kept in an environment that is dry and free from any particles that could alter the quality or structure of the chemical.
  • Peptides should remain frozen until they are to be used to extend the shelf life of the product. The use of a frost free freezer is not commonly recommended for storing peptides as these machines greatly alter the temperature and moisture levels within the storage facility that can have a negative impact on the delicate peptides which are being stored here.
  • If you are working with a new peptide supplier, ask what precautions are taken to ensure stability of the product during shipping. Short term changes in temperatures or moisture levels can have a disastrous effect on the stability or the safety of peptides that will be used in research settings. The best peptide suppliers have taken these concerns into account and will use temperature controlled settings in every environment where a peptide is produced, packaged and stored– to ensure maximum stability and quality of product for the research facilities that will receive these shipments.
  • Peptides can be kept in cold storage for up to two years if they are kept sealed, dry and at around -20 degrees Celsius. Once it comes time to use these peptides in applications to animal test subjects, they will need to be slowly brought to room temperature and reconstituted. The specific methodology used for this process will vary, based on the methods that were used to create the original peptide. Instructions for reconstituting, including the liquids intended to be used for this purpose, should be outlined in the packaging of the peptide that was received with the initial purchase.

Those that are planning long term research should only measure out the amount of peptide they require for a given application, then quickly reseal the container and return it to the freezer for safe keeping. This will help to ensure consistent results in future applications.

Selecting a Supply Company

The best peptides for use in a research setting must be carefully prepared in order to ensure that they will provide uniform results and minimize negative reactions from the animals that are being used to test these reactions.

  • Bulk peptides are typically purchased by researchers to ensure they will have enough supplies to run multiple trials of an experiment. It is not uncommon for experimentation to require the application of a peptide one or more times a day for a month or more in animal test subjects, which will require a great deal of supplies on hand to ensure that the experiment can be continued on a planned schedule.
  • When they are produced properly, buying peptides in bulk can ensure consistency that will help to narrow down the types of reactions that peptides can cause when administered to animals. This is particularly helpful as researchers work to better understand the effects of peptides that have been altered to better suit the future needs of the pharmaceutical industry. This includes peptides that have had a preservative agent added to the formula or those whose bonds have been shortened or otherwise altered to increase their half-life—both on the shelf and in the animal’s bloodstream after application.
  • In order to ensure the highest quality product for peptides are available for research, restrict your use to peptides that were produced in the United States. These peptides were created using consistent methods and are designed for research that is being done through United States pharmaceutical industries. This means that all peptides have been set to ensure the highest possible level of safety for animal test subjects and are created and stored in a way that ensures they will be sterile when applied to a research setting.

Maxim takes great care to ensure that all peptides they produce and sell are research-grade quality. This includes creating a bulk sized batch that is high enough quality to run multiple trials without the risk that the peptide will break down prematurely and begin to produce alternate results than those that are predicted.

This also means that all peptides produced and sold from this manufacturer were created in a sterile environment and designed with the intention of being used on animal test subjects, further ensuring that there will be no unexpected side effects or risks that could jeopardize the integrity of a research project.

Given the vast amount of reactions that have been seen between peptides and animal tissues both from natural peptides that are produced by animal’s body and those that have been applied to animal tissue via injection or other means, there is much variety in the peptides that might be appropriate for a research setting.

Scientists will frequently purchase a variety of peptides that have a similar function and compare their reactions against each other as a means of better understanding how these peptides react against bodily tissues in animals, particularly when they are synthetically made or applied externally.

 

Resource Box:

http://extremepeptides.com/blog/best-peptide-supplier/

Which Polymers Code for an Organism’s Traits

Posted on December 24, 2013 by Maxim Peptide Posted in Peptide Research

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Proteins are responsible for coding an organism’s traits. A genetic code will define how sequences of nucleotide triplets known as codons will determine the sequence of amino acids during protein synthesis. In general there are three nucleotide codons in nucleic acid sequences that will create one amino acid, though there are some exceptions to this rule. Most genes use the same RNA codon table to create these patterns, known as the standard genetic code, which is altered based on the specifications needed for a given organism.

Not all genetic information is transmitted or stored within the genetic code. DNA contains sequences that can be used for regulating this process as well as chromosomal structural areas, intergenic segments and non-coding DNA that is used to phenotype different types of cells. These elements follow a separate set of rules that is not within the codon amino acid paradigm that helps to regulate the genetic code.

Which Polymers Code for an Organism’s TraitsTransferring the Genetic Code    

The genomes of organisms are typically stored in the DNA, though viruses contain this information in the RNA, which is used to code the proteins for different genes.

  • Genes that are coded for proteins contain tri-nucleotide codons that contain the instructions for an amino acid. Each of these sub-units contains a deoxyribose sugar, a phosphate and one of four different nucleobases, guanine, adenine, cytosine or thymine.
  • The double helix of DNA joins two strands together using hydrogen bonds in a base paring. These bands typically match thymine with adenine and guanine with cytosine. RNA matches thymine with uracil and contains ribose instead of deoxyribose.
  • The coded proteins are transcribed onto molecules with the RNA polymer. In prokaryote the RNA will act as mRNA and ribosomes will act on a chain of amino acids known as polypeptides. This process of transferring RNA to a certain amino acid is powered by guanosine triphsosphate and requires a number of factors to allow for translation. tRNA must be provided with complementary anticodons to the mRNA so it can be covalently charged with the amino acids at their CCA ends by aminoacyl tRNA synthetases. This has a high specificity rate for the cognate amino acids and the tRNA alike which is one of the major reasons why these enzymes are capable of maintaining the translation of the protein sequences.

Different amino acids can be encoded with up to six different codon sequences. This can be compared to using bioinformatics, comparing codons to different words or a piece of data that is necessary to create a whole message. In this example a nucleotide would be a bit, or the smallest possible unit that can be used to make a functional message.

This allows for a wide degree of variation both between different kinds of organisms and within the same species. High amounts of variation ensure that organisms are able to adapt to their environment, helping to ensure survival over time.

Varying the Genetic Code

Slight variations in the genetic code have been predicted as early as 1979 with the study of mitochondrial genes.

  • Since this discovery a variety of alterations to the mitochondrial code, both large and small, have been discovered.
  • Viruses use the same genetic code as the organism that is acting as their host, so being able to predict and modify the genetic code of an organism could interfere with their ability to function. However, there are some types of viruses that are able to work within the modification of a genetic code in their hosts. Some bacteria or archaea use common start codons and alter the proteins used by the species that they invade to get around this as well.
  • Some proteins can be substituted for the standard stop codons depending on how the messenger RNA interacts with these sequences. This allows different codes to be expressed simultaneously in a single organism, creating a difference in their growth conditions. In spite of this, the codes in these organisms will be very similar. All coding mechanisms contain a reading code and tRNA ribosomes that move in the same direction and translate the code into amino acids three units at a time.
  • Given these alterations in coding, 40 unnatural amino acids have been added to the protein sequence to create unique codons since 2001.

Some predictions to the genetic code can be performed if the genes encoded on a particular genome can be identified. If researchers compare the DNA from some amino acids to the proteins in other genomes, they can get an idea of how these traits will be displayed. Evolution conserves protein sequences, which helps make it possible for observers to predict how amino acids will be translated from different codons.

A program called FACIL can be used to automatically predict different expressions of the genetic code by seeking out different amino acids in a homologous protein domain and how they are aligned with the codons.

Mutations and Errors

During DNA replication you may occasionally see errors known as mutations that occur as the second strand polymerizes.

  • Mutations can impact the development of the phenotype of an organism, particularly if the protein code sequence was affected by this change. These mutations occur around once every 10 or 100 million times during polymerization based on the ability of the polyerases to perform this function.
  • If a mutation disrupts the frame sequence it can result in a very difference cell from the original, impairing the protein and causing in vivo alterations in coding. A properly encoded protein sequence is essential for the proper growth of the organism to ensure that it will be able to survive against different challenges it will face in the environment, so alterations in the protein sequence can often result in the organism dying before it becomes viable. Therefore the inheritance of a mutation is quite rare.
  • In some cases a mutation can result in a genetic disease being inherited such as Down’s syndrome in humans. These types of occurrences typically prevent the organism from reproducing, limiting the chances that these traits can be passed on.
  • Some alterations to the protein sequence do not do any harm, or even have a positive effect, allowing the organism to better withstand new changes to their environment or reproduce at a better rate. In this case these traits will be passed on more quickly, causing a change in the population of organisms as a whole. This process is known as natural selection.

Though not always considered a form of life, viruses use this mechanism as a means of survival. Their RNA is capable of mutating very quickly, allowing it to work around the immune system of the animals where it invades. When working with large groups of organisms like E. coli that reproduce very quickly using asexual means a mutation can be helpful for ensuring survival. This is known as clonal interface which causes a high amount of competition in organisms.

There is also a phenomenon known as degeneracy that refers to the redundancy of the genetic code which causes a lack of ambiguity. This may be helpful to an organism if some errors in their genetic code cause a silent mutation that does not affect the structure of the proteins because the overall hydrophobicity or hydrophilicity is kept equal by substituting the position of amino acids. These types of errors can lead to a shared ancestry of tRNA synthetases that are related to the patterns created by the codons.

Resource Box:

http://en.wikipedia.org/wiki/Genetic_code#Transfer_of_information_via_the_genetic_code

Chemical Report 2

Posted on December 21, 2013 by Maxim Peptide Posted in Case Studies

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cjc-1295 online reportThe structure and chemical integrity of a peptide plays a strong role in the way that this peptide interacts with biological components. Peptides may be designed to interact with specific cells or tissues, and are therefore given the opportunity to bond or break—based on the needs of these areas. The way a peptide breaks or continues to bond with structures throughout the body will determine the biological process that is completed as well as the success of this function once it has begun.

The ability to create peptides with sound bonds is essential both to natural peptides formed by the body and synthetic peptides that are applied to animals for research purposes. The sooner a chemical bond within a peptide is broken, the shorter the effective life of this peptide will be.

If a peptide does not have an effective structure, it may be vulnerable to damage on the shelf, which can alter research data or create unexpected side effects in animal test subjects upon the  chemicals being applied. There are a variety of products and chemical methods that are used to address this growing need to ensure that peptides that could one day be used for pharmacological purposes will behave in a consistent manner.

3.5.5 Discuss the relationship between one gene and one polypeptide:

IPam

Ipam is an abbreviation for NNC 26-0161 more commonly known as ipamorelin, a polypeptide hormone that acts as a secretagogue and mimic to ghrelin that was developed by Novo Nordisk.

  • This synthetic peptide was developed in the 1990s as part of a group of peptides designed to mimic GHRPs that are developed within the bodies of animals. Ipam is capable of encouraging an animal’s body to release a large amount of growth hormone without the need for additional peptides to be present. This is because the peptide suppresses somatostatin which normally acts as an antagonist to GHRH and stimulates the anterior pituitary to release growth hormone the way GHRP-6 or GHRP-2 would.
  • Similar to GHRP-2, Ipam does not affect the lipogenic properties of ghrelin, but unlike GHRP-6 Ipam does not induce hunger in the animals when it is applied.
  • Ipam can act synergistically if it is applied while natural GHRH is present in an animal’s system or when it is administered alongside a GHRH analog or GHRH itself. Common analogs include GRF 1-29 or semorelin.
  • The synergy of these peptides stems from the somatostatin suppression and the increase in growth hormone per somatotrope. GHRH increases somatotropes that increase growth hormone but Ipam creases a neuronal excitation of the animal’s hypothalamus that can last up to 3 hours after the chemical is applied. This is a similar reaction to GHRP-2 or GHRP-6.
  • Compared to other chemicals in the GHRP family, Ipam has a unique set of properties known as selectiveness. In one study growth hormone secretagogue acted with an increasing efficiency and potency in vivo and in vitro. This led to the chemical being identified as one of several compounds that lacks the central dipeptide ala-trp that is commonly seen in GHRP-1.
  • Ipamorelin caused growth hormone releases in the pituitary gland of rats in vitro—with a similar potency of GHRP-6—which allowed researchers to profile this chemical as a growth hormone releasing hormone with an antagonist structure that was capable of stimulating growth hormone via the GHRP receptors.
  • Research in pentobarbital rats that were anaesthetized, Ipam was capable of causing a release of growth hormone that was just as efficient and potent as the reaction from GHRP-6. This reaction was once again seen in swine that were conscious during study, with Ipam releasing growth hormone in the plasma at a rate that is quite similar to GHRP-6. However, in this case there was a higher potency of growth hormone when GHRP-2 was applied, though the efficacy was lower.
  • In swine, none of these growth hormone secretagogues affected TSH, FSH, PRL or LH levels in the plasma. Administering GHRP-2 and GHRP-6 increased cortisol and ACTH levels in the plasma but there was no release of ACTH or cortisol levels when Ipam was administered in levels that were 200 times higher than the ED50 for growth hormone release. This research indicates that Ipam would be an ideal candidate for further study for clinical development.
  • GHRP-2 and GHRP-6 are not capable of increasing prolactin or cortisol levels but Ipam can selectively release growth hormone, regardless of the size of the application. Mega-applications of Ipam can create a mega-release of growth hormone which can allow the body to release the entire amount of the hormone currently stored in the pituitary gland of the animal. GHRP-6 and GHRP-2 are only capable of allowing an animal’s body to release around 1mcg/kg of growth hormone regardless of how much of the chemical is applied.
  • The pharmaceutical industry is particularly interested in any research that assists with targeting or identifying the properties of bioactive peptides in more complex matrices. This can help to assess the feasibility of these peptides in supercritical fluid chromatography of the separation of two pairs of water soluble peptides with the same composition, mass and charge which are only differentiated by the sequence of their amino acids. Evaluating a variety of these conditions, including the conjunction of trifluoroacetic acid, may be the most effective model in noting the elution of isometric pairs of peptides in nitrogenous stationary phases.
  • By contrast to this methodology, ammonium acetate and water can create peak shapes in these measurements which are found to be less ideal than additives that are neutral. Basic additives such as iso-propylamine combines with HA-Pyridine can create a high resolution factor that can complete a study on the given peptides. It was found that aminopropyl and HA-pyridine created the best resolution for evaluating these peptide pairs while phenyl-hexyl and silica did not allow for the necessary separation.
  • Carbon dioxide and a methanol modifier have been found to assist with peptide solubility transport with stationary phase solvation while HTFA helped to fully protonate the peptide pairs from their ion pair to conjugate the based cationic peptide analate. This separation process was found to be the ideal ion pair supercritical fluid chromatography for this method with Ipam providing the ideal resolution for HA-Pyridine columns for peptides in a neutral state.

Analytial and preparative scales include supercritical fluid chromatography that indicate a widespread applicability for separating chirals of polar pharmaceutical candidates, but this technique is quickly becoming achiral because there is a larger utility for separating ionic analyates, like organic sulfonates and amine salts.

The key to this is including additives like ammonium acetate and trifluoroacetic in the mobile phase of associating with the stationary silica and evaporative light scattering detection. This method was found to create a .3 TFA in methanol and .2 TFA in 90:10 methanols: water and a spike with a 90:10 ratio of Ipam and methanol.

Protein Synthesis, Translation (1):

Protein Synthesis, Translation (2):

Protein Synthesis, Translation (3):


Insulin Growth Factor

Insulin-like growth factor or IGF most commonly refers to somatomedin C or IGF-1 which is a protein that is encoded using the IGF1 gene.

  • IGF based peptides contain a large group of chemicals that are used in an animal’s body to communicate physiologic environmental changes or needs. To achieve this, IGF molecules have to cell-surface receptors and ligands which are arranged in a variety of ways, allowing for a six-high affinity of binding proteins and IGFBP degrading enzymes, known as proteases.
  • The axis of an IGF molecule is known as the growth hormone/IGF-1axis. IGF-1 is typically secreted by an animal’s liver when it is stimulated by growth hormone and used for regulating the physiology of the body and preventing pathological problems such as cancer. The axis helps to maintain cell proliferation and inhibits cell death when possible.
  • IGF-2 is believed to be a primary growth factor that is essential to the early expression of growth hormone while IGF-1 is used to maximize the growth of tissues. Studies on mice have noted these differences and also helped the scientists to realize that IGF-2 is primarily shown in the fetal animals rather than in full grown animals as a means of developing the kidney, brain or liver.
  • There are systems which can vary the expression of IGF-1 and growth hormone in the circulation. This may include the genetic makeup of the animal, its sex, age, amount of exercise, nutrition level, stress level, disease state, species, body mass index, xenobiotic intake and estrogen status, among others. IGF-1 is found to regulate the development of neurons— including those for synaptogenesis, neurogenesis, myelination and dendritic branching. It can also be seen assisting with neuroprotection after neurons have been damaged. Children with a higher IQ have been found to have higher levels of serum IGF-1.
  • The development of cochlea is also impacted by IGF-1 by managing apoptosis. A deficit of IGF-1 for this system can result in hearing loss. There appears to be a correlation by a lack of IGF-1 and a reduction of hearing and short height in young animals or those entering some form of puberty.
  • There are a variety of types of IGF receptors so it can be difficult to narrow down the distinct types of tissues that are affected by IGF-1, particularly when comparing reactions amongst different species of animals. The role of IGF-1 as a neurotrophic factor is perhaps the most well-known because it is easy to tract its induction of survival neurons. In many animals IGF-1 also causes hypertrophy in skeletal muscle because it induces protein synthesis that can block atrophy. In many cases IGF-1 can also protect cartilage by activating osteocytes that can act as an anabolic factor for bone cells. In very high concentrations IGF-1 can act as an insulin receptor and compliment the effects of insulin that is also present in an animal’s system.
  • The tissues in an animal’s body will display a variety of IGF-1 receptors based on the effects that would best impact this tissue and induce survival of the neurons that are present in this area of the animal’s body. Common reactions that affect this phenomenon include hypertrophy in skeletal muscle, blocking muscular atrophy protecting cartilage and inducing the synthesis of proteins. IGF-1 is also associated with activating osteocytes which could be anabolic in some animals.
  • Both IGF-1 and IGF-2 are regulated by proteins, known as IGF-binding proteins, which are used by animals’ bodies to modulate the IGF receptors that can work both as a means to inhibit IGF by simultaneously promoting the use of IGF in theory by helping the delivery of the chemical to the receptors so that the half-life of IGF-1 is increased. Current data suggests that IGFBPs are essential to the ability of an animal to regulate IGF once it has been activated.
  • Recent studies indicate that the IGF/insulin axis is essential to the aging process. Fruit flies and nematodes amongst other animals show an increase in their lifespan when their version of insulin that mimics the gene in mammals is eliminated. It is somewhat difficult to replicate these results in mammals because the production of insulin is linked to a variety of genes and therefore cannot be completely eliminated.
  • Simple organisms have fewer IGF-1 receptors and in many cases the roles of these insulin types are unknown. This is largely because these organisms lack specialized organs that would require insulin to react as part of a glucose homeostasis reaction. In addition to this IGF-1 has been found to cause dauer formation to developmental stage C in nematodes which will affect the lifespan of the animal when it is in the larva stage, a situation that lacks any correlation with mammals. Because of this lack of correlation between species it is unclear whether or not IGF-1 will perturb aging in mammals though there is some indication that the phenomena may be related to restrictions in the diets.
  • Additional studies are currently ongoing to determine to determine how IGF impacts diseases such as diabetes or cancer. It is currently indicated that IGF may impact the growth of breast or prostate cancer cells though researchers are not currently able to agree how IGF-1 plays a role in this process.

Current difficulties are posed to those that are studying the impact of IGF-1 and IGF-2 and how these things could be utilized in future pharmacological settings because there is such a variance in how these peptides behave in different types of animals.

Today, researchers are not yet ready to begin testing IGF based applications on human test subjects, but the variance of reactions in test subjects such as swine, emus, insects or rats make it difficult to narrow down what types of applications would even be appropriate for human test subjects. In some cases, the use of synthetic human tissues or tissue samples have been helpful in moving around this obstacle until more definitive data can be confirmed.

Structural Integrity of the Blends

integrity of the blendPeptides, both short and long, rely on their natural structural integrity to interact with tissues and complete biological tasks, and this is something that a synthetic peptide will need to address in order to have biological significance.

  • Data from a variety of animals or human tissue samples indicate that the integrity of myelin sheaths will deteriorate during normal aging, which can result in neural networks that are commonly found throughout the body to become disconnected or otherwise disrupted. This phenomenon can be viewed using an MRI, which is typically used as a way of accessing the impact of things such as Alzheimer’s disease on the brain and other neurological tissues. Evaluating the affected tissues early can help to determine the condition of the genu and the splenium to determine both the presence of the disease as well as the most effective means of addressing these complications.
  • Calculating the transverse relaxation rates using an indirect measure of the white matter and the structural integrity of these neurological formations. The relationship between the splenium and genu differed in two main regions of the animal brain. The quadratic function was used to show the accelerating rate of decline in structural integrity starting around 31. The genu was found to deteriorate while the splenium decline was more gradual or liner. This indicates that age related structural damage is heterogeneous and consistent with the myelin properties that are more susceptible to the aging process.
  • The function of the brain and signaling throughout the body is also largely reliant on peptides and the release of hormones stimulated from this chemical for normal bodily function in animals. As the aging process begins to impact the structural integrity of animal tissues, the proper function and integrity of the peptides throughout production may also be impacted. Research into these matters will often focus on developing synthetic peptides that could potentially help avert the damage to animal tissue, as a result of such structural damage from the aging process.
  • Throughout the past decade there has been a distinct increase in the discovery of bacteria that are resistant to antibiotics, organisms that are generally classified as “superbugs.” These bacteria cannot be killed with current antibiotics that are approved for human use, which poses a threat to public safety, resulting in a pressing need to introduce new, effective medications into the market.
  • One potential solution for addressing the growing problem surrounding a lack of credible antibiotics is to generate medications that rely on antimicrobial peptides. These peptides are isolated from living entities which use these peptides to create a defense against bacteria and other organisms that can invade an animal’s body and cause illness. Based on a template of the natural peptide, a variety of antimicrobial cationic peptides can and have been designed to combat pathogens. Each of these peptides can be designed with a diverse structure biologically and chemically, to address specific microbial threats or to be used on different types of organisms for antimicrobial purposes.
  • The key to this research is developing new peptide structures that will mimic the natural peptide so they are not rejected by the body, directly address the threat of the incoming microbe and do not pose a potential for dangerous side-effects once they are applied to the animal. Because of these concerns, few peptides have entered clinical animal trials to date, and had success at this stage. The short half-life of many peptides poses a concern when it comes to applying these peptides or storing them in a pharmaceutical setting for medical use later. However, the wide range of biological activities, structures, activity spectra and mode of action those peptides possess shows potential that these issues will be addressed in time.
  • Self-assembly and mineralization of peptide nanofibers shows some potential to addressing the issue of creating peptides that are capable of maintaining their structures for an increased length of time. pH induced self-assembly has been applied to peptide amphiphiles to create a scaffold of nanostructured fibers that is similar to an extracellular matrix. This allows the nanofibers within the peptide to be cross-linked in a reversible manner to decrease or enhance structural integrity as necessary.
  • After the fibers are cross linked they can be subjected to hydroxyapatite or mineralization directly to create composite minerals that have crystallographic c axes of the hydroapatite are aligned with the fiber’s long axes. This alignment is identical to that which would be seen between hydroxyapatite crystals and collagen in an animal’s bone.

Both long and short peptides are designed to be broken down by the animal’s body as a means of harvesting the chemicals used to create the molecule during biological processes. In some cases, peptides will break down into smaller molecules or peptides that are capable of creating additional processes within the body after their initial task has been completed. Due to this phenomenon, long peptides generally have a more fragile structure than those of the short variety. Understanding where peptides are designed to break and what enzymes or biological interactions can cause damage to the structure of a peptide will help researchers develop synthetic peptides with reinforced or purposely weakened structures that can be used to alter the way the peptide interacts with animal tissues.

Tadalafil

Tadalafil is a PDE5 inhibitor that is researched for its ability to address erectile dysfunction in mammals.

  • Originally tadalafil was developed by ICOS but it is now sold worldwide by Lilly ICOS LLC for research purposes. This peptide can commonly be applied to animal test subjects in 40mg applications for best and most accurate results. In some cases tadalafil will be manufactured as Tadacip when it is manufactured in India or provided in smaller applications.
  • Tadalafil is often sold under the name Cialis or Adcira for its potential in addressing pulmonary arterial hypertension or benign prostatic hyperplasia. This refers to a combination of erectile dysfunction and benign prostatic hyperplasia that have coincided.
  • Penile erection as a result of sexual stimulation is caused by a relaxation of the penile arteries and the corpus cavernosum muscles to allow blood flow to increase to this area. Nitric oxide may mediate this response from the endothelial and nerve terminals to stimulate the synthesis of cGMP in the muscle cells. Smooth muscle can be relaxed by Cyclic GMP to increase the blood flow within the corpus cavernosum.
  • Inhibiting phosphodiesterase 5 (PDE5) can help to increase the function of the penis and its ability to achieve an erection by increasing the presence of cGMP, a process that tadalafil is designed to achieve.
  • Because sexual stimulation must be present to release nitric oxide, the inhibition of PDE5 from tadalifil will not have any sort of effect on the function of an animal’s penis without sexual stimulation of some kind being present, which is why this peptide is currently administered to animals just prior to sexual activity with an increase in application size as the animal becomes tolerant of the substance.
  • This current application schedule would not be effective in a pharmacological setting. Men that would require tadalifil for treatment of erectile dysfunction would need to plan their use of the drug and schedule sexual activities accordingly, which in many cases would not be an effective means in achieving a healthy sex life. To address this problem, clinical trials on animal subjects are currently attempting to determine if it would be possible to create an application of this peptide that could be taken once daily for those that suffers from chronic erectile dysfunction. Some European markets are also attempting to lower the application size of Cialis as a means of allowing humans to use this chemical as part of a therapy for erectile dysfunction, though the product is not yet ready for human use. The potential risks and benefits of these types of applications are currently unknown.
  • A variety of trials have been performed on many types of mammal test subjects to determine the side effects of different sized applications of tadalafil. The most commonly seen irritations include muscle aches, back pain, headache, indigestion, flushing of the skin or runny nose. Most of these side effects are conjectured based on the behavior of the given animal. The effects of tadalafil appear to fade after a few hours, though some side effects appear to last as long as 48 hours depending on the size of the application.
  • The FDA has discovered that applying tadalafil can lead to vision impairment caused by nonarteritic anterior ischemic optic neuropathy in some test subjects. Most animals that showed signs of this development had underlying vascular or anatomic risk factors that researchers were unaware of when the chemical was first applied. Animals that are older or already show signs of coronary artery disease, diabetes, hyperdension, hyperlipidemia or were exposed to smoke have an additional risk for this side effect. Because so few test subjects showed these signs and were exposed to a variety of factors that could have impacted their vascular health, no conclusions were drawn regarding the dangers of tadalafil on NAION. However, because this trend was noted, any similar PDE5 inhibitors that are already on the market for human use are now required to carry a label that warns of this possible association and doctors must discuss this potential risk with erectile dysfunction patients that hope to receive a prescription to manage their condition.
  • In studies tadalafil is commonly compared or introduced with other medications. This can help researchers better determine any risks that may be posed to those using this chemical if it enters the market, particularly if there is success in creating a daily form of tadalafil for chronic conditions. It is currently known that PDE5 inhibitors cause transiently low blood pressure, so it cannot be used along with organic nitrates. Those that are exposed to organic nitrates within 48 hours of an application of tadalafil are at risk for hypotension that could be life threatening. This would be difficult for any humans hoping to use a future daily form of this chemical if they suffered from angina as paramedics would not be able to use many common medications to assist them in the case of an emergency. This issue is one of the concerns that is inhibiting the acceptance of a regular application of tadalafil for humans.
  • Predominantly tadalafi is seen to metabolize with hepatic CYP3A4 enzyme systems. The presence of any other chemicals or existing medications that would induce this type of reaction in an animal has been seen to lower the half-life of tadalafil and create a significant reduction in serum levels. This has been seen repeatedly in animal trials.

When compared to similar PDE5 inhibitors including vardenafil and sildenafil, there are a variety of reactions that differentiate tadalafil. Vardenafil and sildenafil are capable of inhibiting PDE6 which is found in the eyes whereas tadalafil is less effective. Sildenafil test subjects are also reported to be more sensitive to light because of this inhibition to PDE6 and have a blue tinge that other test subjects do not.

Vardenafil and sildenafil are also more effective than tadalafil in inhibiting PDE1 which is in the vascular smooth muscle, heart and brain which increases the instances of flushing, vasodilation and tachycardia in test subjects. By contrast, tadalafil is more effective in inhibiting PDE11 than the other PDE5 inhibitors.

Inexpensive Peptide Supplier

Getting the most for your money is essential when investing in peptides for long term research to ensure that there is an adequate supply of chemicals available for large sample sizes and long term trials.

  • Much of the cost of manufacturing peptides has little to do with the ingredients necessary to create the compounds as great deal of these peptides are created from very basic materials that are readily available. Much of the cost of preparing a peptide for sale involves researching the potential uses of this peptide in the research market. Most companies that produce peptides are also performing trials of their own to determine their functionality and how they impact the biological processes that animals require to produce and maintain healthy tissues.
  • Research into peptides available for sale also depends on creating peptides that can easily be shipped to other research facilities without incident. In animal tissues peptides often have a very short half-life that lasts only a few seconds, just long enough to trigger the necessary biological process, before they are broken down and absorbed by the tissue to take advantage of the nutrients contained in the peptide. In some cases peptides will break down into other molecules that can trigger other biological processes, such as those peptides that trigger muscle growth and hunger, which can impact how a peptide will behave in a research setting. Minimizing this breakdown before the peptide is applied to the animal test subject is essential to getting accurate test results from the product.
  • To ensure that there are minimal side effects or breakdown of the chemicals in a research peptide, many companies have altered the structure of a synthetic peptide compared to the originals. This allows them to strengthen the bonds in these peptides to ensure that they will remain intact in the bloodstream of the animal for as long as possible. Some peptides are also altered from their natural forms to attempt to alter how these chemicals will interact with the tissues. Much of the research on the side effects or reactions to these synthesized chemicals are still unknown, so researchers will need to take care to watch subjects closely to ensure they do not provide applications of peptides that are dangerous and alter the effects of their research.
  • Another method used to protect the integrity of peptides for shipping is by shipping these chemicals in a freeze-dried state. This prevents any breakdown of the chemical for months or even years while they wait to be used, particularly if researchers keep these containers sealed or frozen. Researchers can then reconstitute small amounts of the peptide as necessary for individual applications to ensure that the chemicals are likely to behave consistently between trials. When ordering chemicals that require reconstituting, read the directions carefully to determine the concentration of the peptide. This will help to ensure that the chemicals are at the proper level and blended with the right liquid modifier to get accurate results without side effects.
  • Companies that do not have ongoing trials for peptide research actively on their books are more likely to offer inexpensive peptides than those which are attempting to finish similar research products. Those that are currently performing trials on a given peptide  will need to maintain a higher level of stock to ensure that they have enough to manage their own needs, so will likely sell any additional product they have on hand at a higher price to meet the demand. Comparing prices and maintaining a familiarity with others in the field can help to ensure that a fair price for peptides can be negotiated.
  • Companies that produce peptides in mass quantities are also more likely to offer an affordable price. Not all companies are certified or capable of making consistent batches of peptides in large amounts, so it is important to carefully look into which peptide suppliers are the most appropriate for this task. Most who are capable of supplying large doses of peptides will note this in their name or description so that they can readily be identified. Consult with these companies regarding how much of a peptide it is appropriate to purchase at one time so that freshness can be guaranteed throughout the life of a trial.
  • Investing in a company that promises quick shipping is also considered essential for those that are hoping to save money on investing in research grade peptides. The less time a peptide spends in transit, the longer it will last during the trial process, allowing scientists to perform additional trials for each round of an experiment without the worry that there will be inconsistency or negative side effects that could affect the level of research performed.

Like any product, it is vital for researchers to carefully compare companies before investing in peptides. To ensure consistency in research, scientists are often advised to invest in peptides from the same suppliers so they contain the same preservatives, require the same solutions for reconstitution and are designed to be constituted at the same level. Seeking out a company that is certified to create large batches of peptides and has years of experience can help to ensure that a research facility can continue to get the research products they require.

Some companies are willing to sign a long term contract with a research facility they know will be performing a research project for a long period of time. This helps to ensure that the company will continue to supply regular shipments with a set payment so that researchers do not have to worry that they will have the tools they need to manage their experiment.

Working out a long term contract helps to ensure consistency of product and shipments that is essential to accurate and reliable research. This provides an opportunity to perform multiple trials or mimic earlier experiments to help ensure that the results achieved are accurate and can be used as a benchmark for future assignments.

 

Resource Box:

http://www.sciencedirect.com/science/article/pii/S019745800300232X

http://www.ingentaconnect.com/content/ben/cdtid/2002/00000002/00000001/art00008

http://www.sciencemag.org/content/294/5547/1684.short

http://www.swolesource.com/forum/evolved-research-supply/1589-ipam-basics.html

http://www.sciencedirect.com/science/article/pii/S0021967311003402

http://www.sciencedirect.com/science/article/pii/S0021967312002671

http://en.wikipedia.org/wiki/Insulin-like_growth_factor_1

What is Polypeptide Chain?

Posted on December 19, 2013 by Maxim Peptide Posted in Peptide Research

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Polypeptides are a form of peptide rather than a separate entity. These are developed in the body when amino acids are linked covalently using peptide bonds, typically creating a tripeptide though there are a variety of forms that this chemical can take on. On the end of every terminal is an N-terminal or amino terminal that contains a free amino group. The other end of this carboxyl group contains the C-terminal and carboxyl terminals.

There are no specific rules that divide polypeptides from peptides. These are generally classified by their size, with biologists using the term peptide to refer to smaller chains of amino acids that contain a dozen or less separate amino acids in the chain and polypeptides contain those that are larger.

Polypeptide Chain

Both polypeptides and peptides are generally found in every organism on Earth in a wide variety of organizations based on the type of structures commonly found in the given life form. This includes even the most basic organisms such as bacteria or fungi, though the peptides and polypeptides in these organisms do tend to react very differently than those in plants or animals.

Basic Peptide Bonds

Peptides are created when a variety of amino acids in an animal’s body form bonds, creating a single structure that can interact with bodily tissues as required.

  • As a general rule, peptides refer to a bonded group of chemicals that contain 50 or fewer amino acids. Groups that are larger than this are considered to be proteins. In some cases proteins may break down into peptides as they interact with tissues in the body. Peptides may also bind together to create larger proteins based on the type of reactions that they take part in within bodily tissues.
  • Bonds within a peptide are referred to as amide bonds. These bonds contain a nitrogen, carbon and oxygen atom, in addition to other elements depending on the type of peptide that has been created.
  • Peptide bonds can be organized in one of two ways: a double bond can be drawn between an oxygen and carbon atom with single bonds between the nitrogen and carbon atoms or a double bond can be created between carbon and nitrogen atoms with a negative charge on the oxygen. The difference in these structures is referred to as resonance structures.
  • Peptide bonds are actually hybrids of two resonance structures which are closure to a double bond with oxygen and carbon atoms. This means that this is a more significant contribution to the overall structure of the peptide while the other structure plays more of a supporting role. The bond between carbon and nitrogen does not allow these atoms to rotate in respect to the other.

Peptides naturally contain constraints on how their 3D shape can be formed. Interactions between the amino acids and a variety of chemical groups can help determine what part of the peptide faces into the water and which will face inward.

The shape of a peptide or a protein is critical in determining the ultimate function of this peptide, so research is greatly focused on understanding how these proteins and peptides fold once they are created by the cell, and how their shape alters once they start taking part in biological reactions. Understanding these formations will also allow researchers to bond chemicals accurately to create high quality synthesized versions of these peptides for research.

Commonly Related Polypeptides

Many polypeptides that have been identified as vital to mammals are associated with the pancreas.

  • Neuropeptide Y, a neuropeptide containing 36 amino acids is used by mammals as a neurotransmitter to the brain and nervous system. There are a variety of variations of this peptide in different animal groups, though it is often seen acting from the hypothalamus. This polypeptide is produced by the neurons of the sympathetic nervous system to grow fat tissue and act as a vasoconstrictor. In some animals this peptide may be used as means of controlling food intake, storing fat for energy, reducing the perception of pain, controlling blood pressure, controlling seizures and managing the circadian rhythm.
  • Peptide YY or peptide tyrosine tyrosine is encoded on the PPY gene as a 36 amino acid polypeptide. It is released by the ileum cells within the colon during feeding as a means of reducing appetite when the body becomes full, though the full function of this peptide is not yet known. PYY is exerted through the NPY receptors to inhibit gastric motility and absorption of electrolytes and water in the colon. It is believed that this peptide may also suppress the secretion of neuroendocrine cells in the colon and ileum after a meal by slowing gastric emptying.
  • Pancreatic polypeptide is secreted by the endocrine pancreas PP cells. These are predominantly located in the head of an animal’s pancreas. This polypeptide also contains 36 amino acids and is used as a self-regulation mechanism for controlling the secretions of the exocrine and endocrine while also helping to control hepatic glycogen levels from gastrointestinal secretions. This secretion mechanism is found to increase after an animal exercises, fasts or takes in protein, though it decreases when an animal’s body secretes somatostatin or intravenous glucose.

These peptides may take on a variety of other forms depending on the animal where the peptide is formed. This has led to some difficulties in creating a concrete identification process for polypeptides in this family. As a general rule a polypeptide will take on a linear chain format with a singular format, though some peptides are placed into this category if they are particularly long but are not long enough to be classified as a protein in spite of failing to meet these specifications.

Uses in Molecular Biology

Recently peptides and polypeptide structures have been seen additional attention in biology due to their potential in the creation of antibodies that can purify specific proteins.

  • These peptides can be synthesized using antigenic peptides within the desired protein, which researchers use as a means of mimicking antigenic peptides from a desired section of a protein. This has been used to create antibodies in mouse and rabbit test subjects.
  • Peptides are also being used to better understand protein structures and their function because probes can see the structure of these chemicals more easily.

Peptides are also being researched for their inhibitory properties which may have potential in restricting the growth of cancers and similar diseases. In animal test subjects peptides have shown promise in detecting and targeting items such as LHRH and regulating the receptors.

This process could be used to treat certain types of cancer, though the process for synthesizing these peptides or applying them in a pharmaceutical application is still being investigated for its potential methodology. Protein tags that can be used to identify the protein structures involved in this process are still being investigated to better understand how this process works in the body naturally.

The sequences of amino acids in polypeptides are controlled by codons which are located in the mRNA molecules that were used by an animal’s body to translate the polypeptide when it was originally created. This sequence of codons within the mRNA sequence is also dictated by the codons in the DNA that was originally used to transcribe the mRNA that controls the peptides. This helps to keep a great deal of control over a class of chemical that is otherwise highly prone to alterations.

An interesting video:

Resource Box:

http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/P/Polypeptides.html

http://en.wikipedia.org/wiki/Peptide#Pancreatic_polypeptide-related_peptides

Research Liquids

Posted on December 16, 2013 by Maxim Peptide Posted in Peptide Research

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peptide synthesis

Research liquids may be used for a variety of purposes when performing research on organic peptides. In many cases these liquids are used to reconstitute peptides as a means of applying them to animal test subjects so that researchers may gauge the reactions of these chemicals on the natural tissues they interact with. This helps researchers better understand the natural purposes of these peptides within an animal’s body as well as how applying peptides from an outside source could be used to trigger reactions from a variety of tissues.

Peptides within the body are bound as individual molecules which can be sent through the bloodstream to interact with different tissues as an animal’s body demands. This can be used to create a variety of processes which are triggered by a variety of hormones and nerve signals within the body. When used in research purposes, animal tissues will not be given the signals from nerve endings or glands that would normally trigger this reaction.

To ensure that research peptides can move directly into the bloodstream, they will often be applied in liquid form. Placing a peptide in the proper liquid can help to extend its half life and work to ensure that it will react to the right tissues, as it moves through the body following an application.

Common Liquid Research Products

A variety of products are often used as a means of creating a peptide reaction in a research environment.

  • Many liquids are developed with ultrafine magnetic particles that can expand the range of peptides suitable for selling in liquid form.
  • Liquid peptides may be sold in bulk containers or in individual marked research tools for individual applications. The latter is often reserved for larger test subjects.

Common peptides sold in liquid form include, but are not limited to, fragment 176-191, ghrp-2, ipamorelin, igf-1 des and others in the igf family. These peptides have been developed to have superior stability that prevents the need for lengthy reconstitution.

Reconstituting Peptides into Liquid Samples for Research

Generally, peptides that are ordered in bulk for use in research settings are purchased in a solidified state and then set in a liquid state for applications for medical research purposes.

  • Maintaining peptides in a freeze-dried state helps to ensure that they will endure transport with a lower risk of damage. Storing peptides in a freeze dried state also helps to preserve the shelf life of the product, particularly if the samples that are not currently being used are kept in a freezer until they are ready for use.
  • In order to apply a peptide to an animal test subject it will need to be reconstituted into a liquid state. This allows researchers to apply the peptide directly into the bloodstream or the tissue they are hoping to monitor for effects.
  • The liquid used to reconstitute the peptide as well as the amount of liquid used will help to control the size of the application of the peptide. Researchers can use this as a means of altering application size for different types of animals and determining any side effects or unexpected reactions that may stem from the use of the peptide.
  • Most companies that manufacture peptides for research settings will carefully specify the research liquid that is to be used to reconstitute a peptide as well as the amount that is expected to be used for individual applications. If this was not specified in the shipping details before the peptide was purchased it should be noted on the storage container for the peptide.

Like the peptides used for research, the liquids used in creating applications of peptides should be sterilized and kept in a secure location that will help to prevent the breakdown of samples. The research facility that provides samples of the peptides should provide any necessary instructions for how long a sample can be used after it was reconstituted to ensure that it does not begin to break down.

Benefits of Working with Maxim

When purchasing liquid peptide solutions for research settings it is essential to work with a company that will provide high quality items that are suitable for the delicate setting associated with animal research.

  • Any research liquids that are to be applied to an animal test subject must be sterile in order to ensure that there will not be additional side effects during the experiment that cannot be accounted for. Not all research companies create peptides that are designed to be used in a research setting, which means they cannot be guaranteed to be sterile. This should be investigated carefully before investing in any type of peptide for research settings to ensure that you are investing in peptides that are specifically designed for this concern.
  • Research for pharmaceutical work with peptides will typically require several trials or ongoing applications of peptides. To ensure that this can be managed properly, research venues will often order peptides in bulk. To ensure that these peptides are suitable for these types of applications, peptides should only be purchased from a company that is set up to create bulk batches of the peptide you require. This ensures consistency in applications to better determine how these peptides will affect animal tissue or whether or not they are capable of creating the effects researchers are attempting to elicit.
  • Companies that specifically design peptides in bulk will often have a longer shelf life than those that were created for individual applications because they have been stabilized. This can be done by adding a research liquid that can help for the molecule to maintain its structure or by strengthening the bonds within the artificial peptide. If this will make a difference in the type of application you plan to attempt, read the description of the peptide carefully to better understand how the peptide was formed. This can help to ensure that all factors can be controlled with precision during any experimentation.
  • Any companies that are not producing chemicals for specific research use may not take these factors into account. If a website does not offer the information necessary to make an informed decision about how these chemicals were formed or should be used, then they cannot be considered a viable source for research materials.
  • Similarly, peptides must be carefully stored and reconstituted as a means of creating the proper reactions within an animal without overdosing or excessive side effects. A high quality peptide research facility should work to ensure that researchers are well aware of how the liquid was designed to be stored and how long the peptide will last before it becomes unstable.

Maxim specifically designs their products to be suitable for research purposes. Every product has been carefully designed to ensure that they will provide materials that have maximum stability and top performance with minimal risks to any live animal test subjects used. This includes providing any essential information regarding proper application size or storage for researchers.

Peptides generally have a very short shelf life, and also naturally have a short half-life after they have entered an animal’s blood stream. A peptide manufacturing company will often make adjustments to research liquids and peptide bonds to help prevent the premature breakdown of these substances that could limit quality research. Pharmaceutical research companies are often interested in how such changes would impact the functionality of the peptide application to better determine if these altered chemicals could have a future in a pharmaceutical setting.

Resource Box:

http://www.grc.org/programs.aspx?year=2013&program=liquchem

Peptide Research

Posted on December 13, 2013 by Maxim Peptide Posted in Peptide Research

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Peptide Research

Peptides are amino acid chains that are developed by creating amide bonds, more commonly referred to as peptide bonds given their prevalence in this structure. If these chains form enough bonds and create a large enough structure they can create proteins, which are found in all forms of life on Earth. Different types of proteins and peptides are found in different types of organisms, and in some cases the same peptide may be found in a variety of species but take on different reactions based on the physiology of the organism. While the term peptide is commonly reserved for smaller amino acid chains, they may be referred to as glutathione or small tripeptides when referring to chemicals specifically created naturally within the human body.

There has been an increase in the focus of peptide research in recent years. While initially research surrounding peptides focused on identifying peptides present in animals and their natural reactions.

As researchers worldwide are developing an increased understanding of which peptides are present in a variety of species and how these reactions can be triggered with a variety of applications, research is being altered to better understand how harvesting and applying these peptides to an animal without a stimulus within the body will affect bodily functions. This is performed both by harvesting peptides from an animal’s blood stream after they are triggered and creating a bonded chemical which mimics the structure of a natural peptide.

Storing Peptides during Research

Long term storage of peptides during research should be undertaken with great care to ensure the stability of the product, maximizing the potential for uniform results throughout the testing period.

  • In general, long term storage of peptides is somewhat problematic as peptides are designed to break down for use in a variety of bodily functions when they are exposed to the elements, or exposed to bodily tissues after application. Many peptides have been altered to increase stability both during storage and after application; though these altered peptides may show alternative reactions to their natural counterparts.
  • In general, lyophilized peptides have higher stability than other types of chemicals, which makes these ideal for research that will be ongoing for years at a time. Lyophilizates can be stored for years if kept at -10 degrees Celsius or lower with no signs of degradation. However, once these peptides have been reconstituted into a solution their stability is significantly more limited.
  • Peptides are susceptible to degradation when exposed to any items of bacterial or protease origin, so a filtration system used after reconstitution increases the risk of damage to these solutions. Any peptide solutions used should be carefully stored in containers that have been sanitized to further reduce the risk of degradation before they can be applied to animal test subjects. Sterilized water is an ideal material for reconstitution for this reason.
  • Peptides that contain residues of tryptophan or methionine are at risk for oxidation which can cause impurities even if the solution is not exposed to microbial agents. In order to reduce or eliminate this risk, peptides that contain these amino acids should be reconstituted using oxygen free solvents.

When determining the pH of the peptide solution for application in animal test subjects, most peptides will maintain more stability when kept in an acidic environment. It is generally recommended to mix peptide solutions at a pH of 3-6 but solutions of peptides that are frozen in aliquots should be subjected to as few freeze-thaw cycles as possible. Reconstituted peptides should also be relyophilized to help ensure the highest level of stability possible.

Peptide Reactions in Female Test Subjects

Many peptides have been used in research for building muscle and increasing the size of an animal which naturally lends itself to male physiology, but new research is attempting to understand how these peptides affect female physiology as well.

  • Many peptides are designed to create a pulse of growth hormone in the body which can then be controlled to create reactions within the animal. Male animals have three main growth hormone pulses from their pituitary gland, the largest of which occurs at night. With a basic understanding of this, researchers are able to stimulate or manipulate these pulses to create reactions as desired.
  • Female animals appear to have a continuous amount of growth hormone in their system with slightly elevated levels in the plasma. Therefore, many of the methods used in traditional research, stimulating the pituitary gland to create bursts of growth hormone are largely ineffective when applied to female animal test subjects.
  • Only certain peptides have been found to be particularly effective in creating reactions in female test subjects if the ultimate end goal is to create substantiated growth. The first is conjugated CJC 1295, an hGH secretogue that contains an additional lysine molecule that will help with facilitating a DAC complex so that the peptide has an 8 day half-life.
  • A single application of CJC 1295 has been found to mimic the normal growth hormone pulsate cycle of a female animal by signaling growth hormone releasing hormone to increase the amount of peptide that individual cells secrete.
  • The second peptide that appears to be effective in working along with the natural female growth hormone cycle is GHRP-based peptides, particularly ghrelin or GHRP-6. These peptides can act on different somatotrope cells which are responsible for releasing growth hormone by increasing the number of these cells that are releasing growth hormone at any given time. This will not increase the amount of growth hormone that is produced by the cells like CJC 1295, so these peptides may be applied to animal test subjects simultaneously if need be.

There are a variety of other peptides that are regularly applied to female animals in addition to these two peptides. Much of this research focuses on the differences in reactions that are seen when these peptides interact with an alternative growth hormone cycle. Some peptides are also designed for use in vivo or in vitro which helps to eliminate the difference in reaction that could eliminate the effectiveness of peptides in other circumstances.

Creating Research Solutions

When reconstituting a peptide, care should be taken to ensure that the proper environment is created to stabilize the product.

  • In general, peptides can be mixed with bacteriostatic water without risk, though peptide manufacturers will typically specify any additional liquids that are recommended for this purpose. There is one exception to this rule, as IGF peptides should only be reconstituted with acetic acid.
  • Peptide solutions can be made stronger or weaker as necessary based on the amount of liquid that is added to the syringe prior to the application. As long as the total amount of the solution is not changed throughout the application process there should be no alteration in the behavior or stability of the chemical.

Peptide solutions are typically measured using micrograms, which should remain constant throughout the application process. Any peptide solutions should be kept refrigerated until the moment they will be applied as these solutions begin to lose stability rapidly after they are reconstituted.

Most solutions cannot last longer than 2 weeks in this state, but the vial should contain any instructions regarding how long they should last and what sings you should check for before applying the solution to an animal test subject to ensure that the peptide will behave as necessary for the nature of your experiment.

Resource Box:

http://onlinelibrary.wiley.com/doi/10.1034/j.1399-3011.1999.00123.x/abstract

Igf-1 Protein

Posted on December 10, 2013 by Maxim Peptide Posted in Peptide Research

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Igf-1 ProteinIGF-1 stands for insulin-like growth factor 1, which is often sold under the name somatomedin C. This is a protein that is encoded by the IGF1 gene in humans, though it is seen in other forms in a variety of types of animals. This peptide is commonly referred to as the sulfation factor which creates non-suppresible insulin-like activity.

IGF-1 has taken on this name because it is has a molecular structure that is very similar to insulin and acts in a very similar way to this chemical. Natural versions of IGF-1 contain 70 amino acids that are aligned in a single chain.

IGF-1 is largely produced in the liver with endocrine hormones and can target tissues using autocrine and paracrine mechanisms. This is stimulated by growth hormone, though can be limited by a lack of growth hormone receptors, under nutrition or failure of the signaling pathways downstream of the signaling pathway. IGF-1 is almost always bound with the binding proteins of IGFBP-3 which is one of the most abundant proteins in this synthesis.

In rats IGF-1 was found to be associated with dietary casein and having a negative association of protein-free diets. Plants have been found to contain biologically active recombinant IGF-1, which was noted in transgenic rice grains.

Role in Muscle Repair

New studies have indicated that IGF-1 is vital to repairing and regenerating muscle tissue in animals.

  • Skeletal muscle is a highly dynamic tissue that is designed to respond to external and endogenous stimuli which includes mechanical loading, growth factors and alterations. Soleus muscle in particular is found to express muscular atrophy then the muscles are not used or extensively damaged.
  • IGF-1 has been implicated as a regulator in muscle modulation and repair, including controlling muscle size in animals. This was examined for a viral mediated overexpression of this peptide on soleus muscle following the immobilization of the hind limb upon reloading in mice.
  • During this process recombinant cDNA viruses containing IGF-1 were injected into the posterior hind limbs of the test subjects and the contralateral limb was simultaneously provided with an application of saline.
  • At 20 weeks the hind limbs of the mice were immobilized for two weeks as a means of inducing atrophy in the ankle plantar flexor and soleus muscles. The mice were then allowed to reambulate and the recovery of these tissues was monitored for up to 21 days.
  • Initial findings revealed that overexpression of IGF-1 were attenuated with the reloading induced damage of the soleus muscles. This was used by the mouse’s body to accelerate regeneration to force recovery of the muscles. MRI scans of the nice also showed that markers of muscle damage were lower in those that were injected with IGF-1 in the soleus muscles at the 2-5 day market after reambulation.

The reduction of the prevalence of damage to the muscles after an application of IGF-1 was confirmed via histology. This showed a lower fraction of abnormal muscle tissue in the areas that were exposed to IGF-1 2 days after reambulation occurred.

The evidence that IGF-1 assists with muscle regeneration showed timely increases in the central nuclei including a paired box transcription factor, elevated MyoD mRNA and embryonic myosin. This helps to demonstrate that IGF-1 may have potential in protecting skeletal muscle from damage by increasing regeneration and repair of the tissues.

Mechanism of Action

The actions of IGF-1 are primarily mediated by the receptors it binds to, allowing it to interact with a wide variety of tissues and cell types in animal bodies.

  • Binding to different activators of AKT signaling pathways can stimulate cell proliferation or growth. It is also found to be a mediator of growth hormone effects from the anterior pituitary gland, which in turn moves from the bloodstream to the liver to trigger the production of IGF-1. It has also been seen to inhibit programmed cell death.
  • Animal tissues throughout the body in a variety of different species have been found to interact with IGF-1 including cartilage, skeletal muscle, kidneys, liver, skin, nerves, lungs, hematopoietic cells and others. This peptide can be used to create effects similar to insulin, control the development and growth of cells and synthesize DNA. This is particularly seen in nerve cells.
  • Deficiencies of IGF-1 or the presence of growth hormone have been shown to cause animals to display a diminished stature, though supplying animals with recombinant growth hormone or IGF-1 in clinical trials has been found to help increase their size. Researchers hope to continue to research this potential to develop a treatment for plan for conditions such as Laron syndrome. Research has also been found to improve these conditions in cattle and IGF-1 has been found to help improve reproduction in these animals.

IGF-1R and growth factor receptors can be triggered using multiple pathways. PI3K has been found to be an influential downstream partner in mammals, acting as a target for rapamycin. The full interaction of these receptors is still being investigated.

Receptors and Binding

IGF-1 has been found to bind with two surface receptors, though research is still ongoing to determine other connective points.

  • IGF-1 may bind to insulin receptors as well as IGF1R. The latter appears to have physiologic effects that have an increased affinity for IGF-1 rather than those that are bound to the insulin receptors.
  • Both of these receptors are a tyrosine kinase that causes phosphate molecules to be added to certain tyrosines. IGF-1 will also activate insulin receptors at around .1 times the potency of insulin. Part of this signaling response may be caused by IGF1R insulin receptor heterodimers that bind with insulin 100 fold less effectively. This has not been shown to correlate with the true potency of IGF-1 in vivo. This is also not effective in inducing phosphorylation of insulin receptors.
  • IGF-1 production is seen throughout an animal’s life but production is highest during an animal’s pubertal growth spurt with levels gradually reducing as the animal reaches old age.
  • Other IGFBP molecules take on an inhibitory role when interacting with these peptides. IGFBP-2 and 5 can bind with IGF-1 with a higher affinity than the bindings at the receptors. This is used by an animal’s body to increase serum levels of these chemicals to decrease the activity of IGF-1 when there is no longer a need for this peptide.

IGF-1 has been found to be closely related to IGF-2 which can bind with the same receptors, though IGF-2 can also bind with IGF-2 receptors. IGF2R receptors do not have the signal transduction capacities that allow it to sync with IGF-1 to make this protein more available, so it will often bind with IGF-1R.

Like the name implies, IGF-1 is related to insulin due to its structural properties. It is capable of acting with insulin receptors though it is not nearly as effective in this capacity as traditional insulin. Splice variants of IGF-1 are identical at the mature region but have different E domains as MGF.

IGF-1 is found to be naturally prevalent as animals are developing the proper tissues and structure the animal’s unique physiology requires. This peptide is also found to be used by adult animals for anabolic mechanisms. Synthetic versions of IGF-1 have been found to have a mecasermin that has potential in managing growth failure, though research is still ongoing to determine the best ways of utilizing this property.

Resource Box:

http://en.wikipedia.org/wiki/Insulin-like_growth_factor_1

Cytoplasm Animal Cell Function

Posted on December 7, 2013 by Maxim Peptide Posted in Case Studies

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Cytoplasm Animal Cell FunctionCytoplasm contains a gel substance called cytosol that is contained within a cell membrane and organelles of animal cells of sub-structures. The contents of any prokaryote organisms that do not have a nucleus will be housed in the cytoplasm, but eukaryote organisms that have a nucleus will separate this material from the cytoplasm in an area known as the nucleoplasm. In most cases the cytoplasm is 70-90 percent water and is a colorless material. Cytoplasm can be jelly like or liquid, though this depends on what type of cell it is in and how that cell is designed to interact with the body.

Most cellular devices occur within the cytoplasm including the metabolic pathways such as cell division or glycolysis. Granular and inner mass known as the endoplasm as well as the clear, glassy outer layer known as the cell cortex and ectoplasm are controlled within the cytoplasm. Movement of calcium ions throughout the cytoplasm are believed to signal metabolic processes and activity in animals. The movement of the cytoplasm around the vacuoles, a process known as cytoplasmic streaming, is used to signal this process in plants.

Constituents of the Cystoplasm

Cytoplasm contains three major elements that are used to signal its effects in different parts of the cells.

  • Organelles, or the membrane bound structures within the cells are given specific functions that contribute to the larger functionality of the cell. Major organelles such as the endoplamic reticulum, mitochondria, vacuoles, Golgi apparatus, lysosomes and chloroplasts in plants can be suspended in this area of the cytosol.
  • Cortosol is contained in cytoplasm that is found within organelles that are membrane bound. This can make up almost 70 percent of the volume of a cell and contains organic molecules, salts and water. Because the network of fibers and dissolved macromolecules including proteins is very high in cortisol, macromolecular crowding can occur here if the cortosol is not at an ideal solution. This can alter how the components interact.
  • Cortosol is made from a combination of dissolved molecules, cytoskeleton filaments and water, though it also contains the protein filaments that create the cytoskeleton and structures including the ribosome, vault complexes and proteasomes. The fluid portion of this type of cytoplasm is known as the endoplasm.

Cytotoplasmic inclusions, small insoluble substances that are suspended within the cytosol are included in a wide variety of cell types in animals as well as silicon dioxide and calcium oxalate in plants which can be converted into glycogen, starch or polyhydroxybutyrate for energy.

These are commonly seen as lipid droplets that are made up of lipids and protein that can be stored as sterols or fatty acids that are used for energy. These lipid droplets are a majority of the adipocyte volume in cells that are specially designed to store lipids, though other cells may hold these as necessary.

Viewing Cystoplasm at a Microscopic Level

Because cells are too small to be seen by the naked eye, there is no way to observe or understand cytoplasm without viewing it through a microscope lens.

  • Unlike the organelles of a cell, the cytoplasm does not take on any particular shape or function that can be distinctly recognized, but rather helps to make up the body of the cell which provides additional structure for the vital portions of this body.
  • When viewed through an electron microscope the cytoplasm of the cells can be viewed in intimate detail. Animal cells can be seen as a three dimensional shape that contains strands of protein set in a lattice pattern. This is known as the microtrabecular lattice that is designed to interlace with other structures in the cytoplasm to hold other structures in place. This discovery helped scientists to realize that the cytoplasm was not actually a solid mass, but a group of lattes that are interconnected to create something of a fence that would hold together the rest of the cells and prevent the organelles from shifting.
  • The cytoplasm contains a cytoskeleton. Not only does this help to provide a shape for the cell but these cytoplasmic filaments help the cell to move as necessary. The alignment of these filaments will vary based on the needs and shape of the given cell.
  • The cytoplasm can also contain a variety of salts that are capable of conducting electricity. A cell can use these properties to power the mechanics of the cell as necessary. This function will vary based on how the cell interacts with the rest of the body and the specific task the cell is desired to take on.

In addition to helping to provide structure for the cell, the cytoplasm can be used to dissolve waste and nutrients. The cell can use these filaments to move and move materials throughout the cell by using cytoplasmic streaming, a process that creates a churning motion within the cell body. The nucleus is capable of changing the shape of the cytoplasm, flowing throughout the mass as the cell moves.

Research and Potential Controversies

Cytoplasm and many of the known organelles in a cell are designed from maternal gamete which is still being researched for a full understanding of its functionality.

  • There is not a great deal of existing research on the maternal inheritance and cytoplasmic inheritance of mitochondrial DNA compared to genomic DNA or that shared within the cell nucleus.
  • Many traits or items within a cell that have been labeled as female have not been researched to their full extent. The cytoplasm is one of the objects that has fallen into this category, with the nucleus being labelled as male and therefore receiving more attention from researchers. This is similar to the sperm and egg being gendered in a full sized animal body. It is generally believed that both the cytoplasm and the nucleus are essential to creating new life through cell division.

Much of the older information surrounding the cytoplasm was based on the idea that it was a passive part of the cell, existing to provide structure for the active elements that encouraged cellular behavior. This outdated understanding of the cytoplasm has been replaced as scientists have discovered that the cytoplasm is used to encourage viscoplastic behavior. This helps to move nutrients in and out of the cell to fuel the other organelles.

This also helps to move the cell as necessary throughout the body so cells may interact with one another. The reciprocal rate of broken bonds within the cytoplasmic network that helps to create these reactions can be measured and reported, creating a better understanding of the different functions of a variety of types of cells within an animal.

Cytoplasm may also be referred to as protoplasm, or the plasma membrane that surrounds the contents of a cell. This is a generalized term for the water, amino acids, ions, nucleic acids, lipids, proteins and other items that make up this substance. Cytoplasm is more often used to describe the protoplasm in eukaryotes. It is believed that eukaryotes contain a protoplasm that is divisible into a cytoplasm that provides structure and is controlled by the nucleus of a cell that has developed electron microscopy.

This was originally believed to be because cytoplasm was a homogeneous fluid that simply existed to help cells maintain their shape, but it is now known that cells contain a variety of substances and organelles that assist with the functionality of the cell.

 

Resource Box:

http://en.wikipedia.org/wiki/Cytoplasm

http://www.fi.edu/qa97/biology/cells/cell3.html

http://en.wikipedia.org/wiki/Protoplasm

Chemical Report (November 2013)

Posted on December 2, 2013 by Maxim Peptide Posted in Case Studies

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chemcial reportChemicals within the body pose an interesting challenge to researchers that have been tackled in a variety of ways throughout the history of biochemicals. Chemicals within the body contain the same elements and atomic properties that they would in any other setting. However, within organic tissues chemicals take on a unique roll that is not seen anywhere else in nature. These chemicals not only help to compose natural tissue, they are produced by natural tissue to provide a variety of functions that are essential to the function of the body as a whole. What continues to prove to be a challenge for scientists is the fact that chemicals do not behave in an identical manner within different animals, in spite of containing the same molecular structure— and in many cases interacting with tissue with the same makeup. There have been a variety of methods used to help better predict molecular behavior so organic chemicals may be better defined. This process starts with creating a failsafe method for identifying and organizing chemicals discovered in organic tissue so they can be monitored and better understood— based on their properties and their behavior. This can also help to structure experiments that will create artificial versions of these chemicals to be introduced to organic tissue, as a means of controlling biological behavior.

Amino Acid Molecular Weight

Amino acids are commonly identified by their molecular weight, as a means of categorizing unknown chemicals along with chemicals that scientists work with frequently.

  • Amino acids are the second largest component of cells for muscle and other tissues, only being surpassed by water. These amino acids can play a variety of roles within the body, but they are most often seen acting in biosynthesis functions or working as neurotransmitters.
  • An amino acid is defined as an organic acid that is formed from carboxylic acid and amine. These are a functional group of chemicals, each with a side chain that can be formed from nitrogen, hydrogen, oxygen or carbon among other elements that can be used as an identifier for the chemical; each of these side chains is unique to the amino acid. These side chains also help to identify the role of the amino acid in an animal as it interacts with organic tissue.
  • To date, there are around 500 known amino acids which are widely classified by weight, but they are also often classified in to gamma, delta, beta or alpha groups— based on their polarity level. Side chains of amino acids are grouped— based on the additional elements that are included in the chain, such as sulphur or hydroxyl. These groups are commonly listed as aromatic, aliphatic or acyclic.

All molecular weights are noted in g/mol

  • Alanine- 89.1
  • Arginine 174.2
  • Asparagine- 132.1
  • Aspartate- 133.1
  • Cysteine- 121.2
  • Glutamate- 147.1
  • Glutamine- 146.2
  • Glycine- 75.1
  • Histidine- 155.2
  • Isoleucine- 131.2
  • Lysine- 146.2
  • Methionine- 149.2
  • Phenylanine- 165.2
  • Proline- 115.1
  • Serine- 105.1
  • Threonine- 119.1
  • Tryptophan- 204.2
  • Tyrosine- 181.2
  • Valine- 117.1

Each molecular weight, also referred to as molecular mass, is the specific mass of a given molecule. This is calculated by adding the sum of the mass for each atom known to be contained in the atom multiplied by the number of atoms in the molecule. Being able to define the molecular mass will help to determine the size of a molecule, which are then classified as a small, medium or large grouping. Small or medium molecules are defined using spectrometry which will help to determine the stoichiometry. This is how amino acids would be defined. Large molecules, such as full proteins, can be defined using a variety of method– such as light-scattering or viscosity.

  • In most cases, it is more appropriate to refer to a molecule’s relative molecular mass because molecules are often given an assumed mass— based on their relevancy to C. Molecular and atomic masses are dimensionless but are measured in Daltons which can help to define the number for a mass of one molecule, when divided by the mass of C. This will help to provide a molar mass for chemicals so scientists are able to work with a unit gram of the substance.

There are 20 amino acids that have been defined as those that play a vital role in the function of an animal’s body. Of these 20, nine have been determined to be essential to the body because they cannot be created by compounds within the body itself, and therefore must be taken in from other substances. In many cases this helps to regulate the diet of an animal because they must consume foods that contain the proper balance of chemicals to create the necessary amino acid compounds. The specific amino acids that are essential to an animal will vary between species; therefore there is a wide variety of dietary needs. These may also change as the animal ages, presenting a more interesting look at the differences in the functions of animals. Understanding the classifications of these peptides will help to better understand which chemicals are being utilized by animals and how they are built or broken down— based on the interactions they have with the natural tissues.

Short Peptide

short peptide

Peptides are groups of amino acids that work to make up different proteins within the body, each of which take on a unique roll when interacting with bodily tissues.

  • Peptides are formed by short amino acid monomers that are linked by different types of peptide bonds to create a chemical chain. When the carboxyl groups of different amino acids interact with each other, it can create a variety of covalent chemical bonds that will join different amino acids together. The number of amino acids joined in this pairing will help to define what type of peptide has been formed: a dipeptide, tripeptide, tetrapeptide, etc.
  • It is important to note that peptides differ from proteins— based on how they function in the body as well as their size. As a general rule a peptide must contain 50 or fewer amino acids in order to receive this classification, whereas proteins will often contain significantly more, or may even be made up of multiple peptides that break off and act independently as the molecule interacts with bodily tissues or moves through the bloodstream. Proteins will also often bind to ligands to create cofactors or coenzymes which can create completely different proteins or grow to create macromolecules that take on a variety of roles within an animal.
  • Scientists are currently working on learning more about the techniques that peptides use that differ from how proteins interact with the body. It appears as though there are size boundaries that help to determine whether or not a polypeptide or a protein may take on a certain role within the body. The specifics of this are still being learned— as many peptides react differently within different groups of tissues or even within different animals that have similar characteristics. It is also not uncommon to see peptides react differently within male or female animals within the same kingdom.
  • If an amino acid becomes incorporated into a peptide it is referred to as a residue because this type of reaction will typically result in the release of hydroxyl— from the existing carboxyl in the amino acid. This will lead to the formation of water molecules every time an amide bond is made. All peptides have this type of reaction, with the exceptions of cyclic peptides. These, instead, create a residue known as C-terminal or the N-terminal—depending on the type of peptide that the chemicals are reacting with and the type of process that is being generated.
  • There are no specific rules that distinguish proteins from polypeptides. In general, a long peptide that contains amyloid beta data can be classified as a protein, but small peptides, particularly those in the insulin family, are rarely reclassified into the protein group.
  • Within the peptide group, peptides are divided into long chain peptides or short chain peptides. Long chain peptides, or ogliopeptides, may be split into shorter peptides as they are used in a variety of processes throughout the body. These are commonly seen within natural substances, creating the various biological processes that are necessary for the functionality of this tissue. When absorbed or created in animal tissue, they will begin to create a variety of new processes that can assist with tissue engineering. The animal’s body will use the various elements used in the chemical bonds of a peptide to repair, enhance or replace biological tissue or functionality as necessary.
  • Short peptides have a similar functionality to long chain peptides, but they are significantly smaller in size. They are sequentially bonded but do not contain any proteins. There is no specific number of amino acids that will allow a scientist to classify a chemical as a short or long chain peptide, though in general those with only two amino acids are placed in the short category.
  • Both short and long chain peptides secrete hormones which can allow an organism to trigger different biological processes within their body. These hormones can also be used to produce different biological processes as necessary. Short chain peptides tend to be more stable than long chain peptides because there are fewer bonds included in their construction, so in many cases these peptides are considered the ideal system for encouraging a biological process that would require longer or higher levels of stimulation to complete. Long chain peptides, instead, are designed to be broken down and absorbed by the affected tissue as the given biological process continues.
  • Because short chain peptides are more stable, they have a longer shelf life, which makes them an ideal source for biological research. Short peptides are also more efficient when they enter an animal’s body, so it is much easier for scientists to track the changes that these chemicals are making in the body. For this purpose, short chain peptides are commonly the ones produced synthetically, as a means of testing the functions or the reactions of these chemicals on the tissues. While long chain peptides are occasionally used for this research, their length often causes them to collapse shortly after being applied to the tissue, which can result in inconsistent results or data during experimentation.
  • Short chain peptide research generally focuses on the idea of being able to create biocompatible materials that will help to reduce the effects of the aging process on animal tissue. Amino acids that are used to create peptides can be harnessed by the body and used to complete biological processes more efficiently. If the body is not producing or being exposed to the necessary amino acids to maintain the tissues, scientists hypothesize that applications of peptides containing the proper amounts of the necessary peptides could be applied as a means of ensuring that the body continued to function at the right level, or even an enhanced level if desired.
  • Short peptides are considered ideal for this potential biological application. Short peptides are often referred to as self-assembling peptides which contain the active motifs that the animal tissue would need to create a variety of processes. The short peptides that are capable of bonding without stimulation are able to replicate information that was created in the animal tissues and independently create or transmit this information as necessary. This allows the peptide to take on a variety of natural processes that do not require them to change their structure or alter their behavior within the body, which can include the stimulation of tissue engineering when the body is going through a period of growth.
  • The idea of generating new tissue by stimulating the body using peptides is only in its initial stages. Both short and long chain peptides are being used to determine the potential effectiveness of this research, but as of today, most numbers that are associated with this practice are considered to be preliminary data that will be used to fuel pharmacological research in the future.

In an even more interesting biological system, it has been shown that peptides may, in some cases, mimic the reactions or processes of proteins in the body, helping the organism perform processes at a higher level of functionality— in spite of the normal regulations that their body may have. Scientists hope to harness this ability and use peptides in pharmacological applications in the near future, as a means of correcting diseases or deficiencies in humans. Research on animal test subjects often revolves around the application of synthetic peptides for this purpose, though this research will continue to be enhanced in upcoming years as scientists continue to understand the role different peptides play in animal tissue and how this reaction might vary if the peptide is synthetic in nature.

Polypeptide Chain

Peptides are divided into a variety of classes— based on the chains that are used to create them and the processes that they take on once they are created or enter an animal’s body.

  • Ribosomal peptides are some of the most commonly synthesized peptides, though they are naturally synthesized from mRNA translations in an animal. These peptides will often reach their mature form by entering proteolysis, which higher organisms will use as a way of signaling molecules with hormones to generate the necessary biological processes the body requires. In some cases organisms can use these amino acids to create natural antibiotics including mocrocins, with the residues of these amino acids being used by the ribosome as necessary to create the biological process involved.
  •  More commonly, ribosomal peptides will enter into posttransitional modifications including glycosylation, palmitylation, sulfonation, phosphorylation or hydroxylation. These are generally a linear process, though some structures have created a lariat bonding structure during a specific set of biological processes. Some animals are able to use these amino acids to create a more exotic reaction– such as converting D-amino acids from L-amino acids to create venom in platypuses. These unique variations of the use of chemicals generate the need for far reaching research into the use of peptides, as every animal may react to the application of a synthetic peptide in a slightly different manner.
  • Nonribosomal peptides are created by enzymes that are unique to that particular peptide instead of by the reactions of a specific set of ribosomes within the body. Glutathione is the most common peptide in this group, which is used by animal tissue to create an antioxidant defense that can be used to help protect the tissues from aerobic organisms. Additional common nonribosomal peptides include fungi, plant or unicellular organism processes that can be used to synthesize modular enzyme complexes which are known as nonribosomal peptide synthetases.
  • Nonribosomal peptide synthetases usually contain a similar structure, but they will take on a variety of different modules to deal with chemical manipulations within the different types of tissue where they have been placed. This also helps a variety of organic tissues creating the necessary bonds to manufacture this product, given the natural properties the tissues possess. Nonribosomal peptides are typically cyclic and have complex structures, but there have been discoveries of linear nonribosomal peptides as well. The bonding of these peptides is commonly compared to the mechanics that are necessary to create polyketides or fatty acids in more complex organisms. It is not uncommon to see the bonding of a hybrid compound of these structures for this very reason. Compounds that were synthesized in this manner include thiazoles or oxazoles.
  • Milk peptides are created with proteins from milk and are broken down using enzymes in the body, typically the enzymes that are used to fuel digestion, to create lactobacilli. This is the bacteria that are responsible for the fermentation process in milk.
  • Peptones are those that are derived from meat or milk products that are digested using proteolysis. These contain small or short chain peptides that can be broken down or absorbed to create spray dried material such as salts, fat, metal, vitamins and a variety of biological compounds. These peptides are considered the essential building blocks that fungi or bacteria will be used to grow within a nutrient media.
  • Peptides are starting to become a prominent field of study within molecular biology for a variety of reasons. The peptides may be used to create peptide antibodies within an animal without needing to purify the protein that is to be used. This can be performed very simply by synthesizing antigenic peptides of the protein or sections of protein the scientist would like to work with. This can then be used to create antibodies against the given protein. Such research is commonly performed on mice or rabbits.
  • Peptides are also becoming a subject of interest for scientists because they are instrumental in the research of mass spectrometry that allows researchers to readily identify proteins based on their sequence or their mass, greatly speeding up the time initial research takes to discover the necessary structures for a biological process. Peptides that are created the most frequently for this purpose include those in-gel digestions which are created after the electrophoretic separation of the given proteins.
  • Research surrounding peptides are often used as a means of studying the function and structure of a variety of proteins. Synthetic peptides are often used as probes to discover where the bonds or interactions between proteins and peptides occur. The bonding of peptides must be replicated exactly, in order to ensure that these biological processes will react the same way they would in a natural setting, which has fueled additional research into the structure of the given peptides, particularly for those processes that require long peptides to complete. In some cases, scientists are shortening or enhancing the bonds on synthetic peptide structure in order to achieve the stability necessary to create a biological process that can easily be monitored or replicated in the tissues.
  • Research into inhibitory peptides may eventually be used in clinical research to help inhibit cancer proteins or those from other diseases. There is a promising application of peptides that may be able to target and inhibit LHRH. In this case the peptides will act as an antagonist that will interrupt the way the LHRH cells can bind to the receptors on natural tissues within the body. Inhibiting these structures could be helpful in managing conditions such as prostate cancer, if research in animal test subjects continues to progress in a promising manner. At this time additional investigations will be necessary in order to determine if peptides truly have attributes that could be used to fight cancer. The properties that have currently been observed by peptides or similar structures are not yet at a point where it can be considered definitive.

As peptides are used by the body, they will be broken down which creates a variety of fragments. Peptides fragments can be used to identify the different proteins that were the source of this chemical reaction and quantify this protein source to help scientists better understand how to trigger these biological processes. In many cases, the products that are commonly used during enzymatic degradation would break down and make use of these peptides that can be replicated on controlled samples in a laboratory setting, but it can be difficult to compare these reactions to paleontogical or forensic samples, because other natural effects can impact or degrade these samples before the process can be accurately observed.

Where to Buy Peptides

In order to continue research into the understanding and potential use of peptides and their components in medical research, scientists will require a steady stream of peptides to work with during their experiments.

  • In order to gain access to natural peptides, scientists will need to be able to control their release in the animal’s body and then harvest the chemicals as a means of further detecting their impact on tissues or other biological processes. This is not particularly practical, as peptides are naturally released in small amounts that are only designed to trigger a specific biological response. Furthermore, most peptides have a very short half-life, causing them to begin to break down almost immediately after being released to the body.
  • To counteract this problem, a variety of companies have begun to create synthetic versions of highly known and used peptides. These peptides are bonded in the same chemical fashion as the original peptide to ensure accuracy when applied during medical research. However, additional research must continue, as some synthetic peptides have been found to react differently than the natural counterpart they have been modeled to replicate. This is largely theorized to be the result of external application of the artificial peptides, which are independent of the chemical and hormonal process that would trigger the use of this peptide in a natural setting.
  • Peptide manufacturing companies will often sell large quantities of these peptides as a means of providing researchers with the samples they require to perform long-term research studies. Acquiring peptides from a singular source is considered ideal or even essential for many researchers because this allows them to guarantee a consistency of product that is necessary for research grade chemical tools. This also helps to guarantee that the bonding and chemicals used to produce the synthetic peptide will match, better ensuring a consistent performance as it is applied to animal test subjects.
  • Much of the concern regarding using artificial peptides in research is ensuring that the product remains stable for as long as possible. This will help to ensure a consistent performance with the lowest possible level of side effects in animal test subjects. Some peptides have been altered as a means of controlling their half-life, to minimize their breakdown during transport or storage. Peptides are also freeze-dried and reconstituted as necessary as a means of ensuring that a premature breakdown will not occur.
  • Any company that is not shipping peptides in a frozen, temperature controlled state runs the risk that their product will become damaged during transit: thus they may not be suitable for research-grade use. Similarly, these products should contain clear instructions for how they should be reconstituted, when they should be used and how they should be stored to ensure a maximum level of efficiency from the product.
  • While a significant amount of care must be put into the transit and storage of these chemicals, peptides are not in fact difficult or costly to produce. Many who overcharge for peptides are simply attempting to take advantage of the popularity of these products in current research fields.
  • Similarly, some companies add binders or preservatives to peptides as a means of lengthening the time that they can be shipped. However, these additional ingredients can interfere with the results noted when the chemicals are applied to animal tissues.

Maxim sells peptides at a reasonable price so it is easy for researchers to get the high amounts of product they require— in order to complete their research fields. These peptides are stored, sealed and shipped in a way that guarantees to preserve the chemical composition of the product. Peptides are also shipped very quickly as a means of ensuring that there will not be a breakdown in the chemical structure before the researcher has been given adequate opportunity to use these products. No additional ingredients are added to any samples during the production processes to ensure accurate research results.

CJC 1293

CJC 1293 is often referred to in conjunction with the similar peptide, CJC 1294 which is commonly synthesized as a means of controlling biological research throughout the bodies of animal test subjects.

  • CJC 1295 is a tetrasubstituted peptide hormone that consists of a 30 amino acid chain. This peptide will generally function as an analog to growth hormone releasing hormone GHRH. ConjuChem of Canada created this hormone as a means of better synthesizing this process. CJC 1295 was created as a means of improving the function of rHGH or GHRH research because CJC 1295 is able to bioconjugate with substances, such as serum albumen, which will increase the half-life of the product as well as the potential therapeutic window. This is accomplished by protecting groups of amino acids that would normally be susceptible to degradation from enzymes within GHRH.
  • By contrast, CJC 1293 is the natural growth hormone releasing hormone GRF or GHRF which is also commonly classified as somatocrinin or somatroliberin. This is a hormone that is designed to trigger the release of growth hormone. This peptide contains 44 amino acids and is produced naturally within the arcuate nucleus of the hypothalamus in an animal. The first indications of GHRH are commonly seen in the hypothalamus between 18-29 weeks of gestation which is used by the body to produce growth hormone and somatotropes as necessary within the fetus.
  • CJC 1293 is released from neurosecretory terminals in nerves which are within the acruate neurons. This peptide is then carried through the hypothalamo-hypopyseal portal system that will deliver the chemicals to the anterior pituitary gland to stimulate the secretion of growth hormone from the growth hormone releasing hormone receptor. CJC 1293 is released in a pulsatile manner which will help to stimulate a similar release of growth hormone.
  • CJC 1293 is also used by animal tissue to promote slow wave sleep in a way that is more direct than some other biological methods. Growth hormone is required for any postnatal growth or any growth of bone tissues. It is also used to help regulate carbohydrates, proteins and the metabolism.
  • If CJC 1293 is bound with GHRHR. It can increase the production of growth hormone, but this is largely due to the fact that the cAMP dependent pathways will be increased as well as the phospholipase C pathways within minor pathway structures.
  • cAMP dependent pathways are initiated by CJC 1293 binding to it receptors which will cause a confrontation with the receptors that activate G alpha subunits within G-protein complexes on the intracellular side. In turn this will cause a simulation of the adenylyl cyclase as well as an increase in the intracellular cyclic adenosine monophosphates that allows any free subunits to translocate to the nucleus of the different phosphorylate and transcription factors of the cAMP response element binding proteins.
  • Together with phosphorlylated CREB and its coactivators CREB binding protein and p300 there is an enhancement of the transcription of growth hormone that allows for the binding or CREB proteins and cAMP response elements within the promoter region of growth hormone genes. This will also increase the transcription of GHRHR genes that can provide positive feedback on this process.
  • Within phospholipase C pathways CJC 1293 stimulates the phospholipase C throughout the By complex heterotrimic G-proteins. The activation of PLC will continue to produce inositol triphosphate and diacylgylcerol which will in turn lead to the release of intracellular Ca that stems from the endoplasmic reticulum. This will increase the concentration of Ca that will cause vesticle which will release the secretory vesticles that contain a premade growth hormone serum. In some cases the influx of Ca will have a direct impact on the cAMP release that will create a distinct reaction that varies from the traditional cAMP dependent pathways that are used by animal tissue to activate protein kinase A.
  • The activation of GHRHR using CJC 1293 is also used as a way to open Na channels by deploying phosphatidylionositol 4 and biphosphate 5. This will cause cell depolarization and this change can cause the intracellular voltage to open and trigger a voltage dependent calcium channel. When this process is completed it can result in a vesticle fusion that will in turn release growth hormone to the necessary stimulated tissues.
  • Additionally, CJC 1293 can be expressed in a way that is demonstrated within peripheral tissues and cells that surround the main site of the hypothalamus. This type of reaction has been seen in gastrointestinal tracts of animals and the epithelial mucosa. In some pathological studies a similar reaction has been seen in the cells of tumors.

 

  • CJC 1293 is a lead compound in a variety of functional and structural analogs including that of CJC 1295. There are a variety of analogs that are used in research chemicals for specific applications that require CJC 1293 to maintain their structure. Semorelin is one of the most common functional fragments of CJC 1293 which is designed to assist with the diagnosis of deficiencies of growth hormone secretions. Tesamorelin is another analog that is designed to help diagnose lipodystrophy in those suffering from HIV with a highly active antiretroviral therapy program. As of 2011, research is focusing on the effects that these chemicals could have on elderly animals before it can be widely used for experimentation or use in humans.

CJC 1293 and the reactions it has within animal tissue are opposed by somatostatin (also referred to as growth hormone inhibiting hormone). When somatostain is released from its neurosecretory nerve terminals which are designed to act as a perinventricular somatostain neuron; this chemical will be carried through the hypthalao-hypophysical portal circulation. This will deliver somatostain to the interior pituitary where it will cease the effectiveness of CJC 1293 and inhibit the secretion of further growth hormone. If CJC 1293 and somatostatin are released alternatively it can increase the pulsatile secretion of growth hormone. A great deal of research is dedicated to comparing these reactions as a means of understanding how to control or replicate  this processes using synthetic versions of these chemicals. With research into peptides and the potential to create synthetic versions of of these materials still very much in its infancy there is a great deal of potential for creating new therapeutic measures that will help to manage a variety of conditions or diseases that damage animal tissues. As researchers grow to understand the functionality and composition of peptides that much better, it is all the more likely that they will be able to create chemical structures that mimic or enhance the abilities of these chemicals to react with animal tissues. Research on tissue samples or animal test subjects currently indicates that there is a promising pharmacological component to these processes that could see use in humans in the upcoming years if all research continues to progress as planned.

Resource Box:

http://www.lifetechnologies.com/us/en/home/references/ambion-tech-support/

http://en.wikipedia.org/wiki/Amino_acid

http://en.wikipedia.org/wiki/Molecular_mass

http://en.wikipedia.org/wiki/Peptide

http://www.maximpep.com/research/differences-between-long-and-short-peptide-chains/

http://en.wikipedia.org/wiki/CJC-1295 http://en.wikipedia.org/wiki/CJC-1293

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