Category Archives: Peptide Research

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The peptide Fragment 176-191 is a modified version of amino acids 176-191.  It is occasionally known as Frag 176-191 cytoplasmic protein 9.5 and gracile axonal dystrophy.  It stimulates lipolysis, which is the breakdown of fats.  At the same time, the peptide slows down  lipogenesis, which is the formation of fatty acids.

Fragment 176-191’s Mechanics

According to scientific research based on animal test subjects, Fragment 176-191 operates by mimicking the process in which natural growth hormone controls fat metabolism, but does so without the adverse effects on cell proliferation or blood sugar.  This process promotes the breaking down of fat.  Additionally, it promotes the expulsion of energy, fat oxidation, and muscle mass.

The result of this process is twofold.  Firstly, it promotes the breaking down of fat.  Secondly, it blocks the configuration of various lipids and fatty acids throughout the body.  The application of the peptide can enhance an animal test subject’s ability to burn through adipose tissue.  In turn, this promotes the subject’s expulsion of energy, fat oxidation, and muscle mass.  Research has also determined that the peptide’s design enables it to be applied to animal test subjects safely.

Because of the fat burning qualities that are associated with Fragment 176-191’s operational mechanic, current scientific research on animal test subjects have primarily been built around researching the peptide’s ability to promote weight loss.  Specifically speaking, the studies have been essentially built on ways that the peptide can be used to imitate the effect of fat reduction when it is introduced into a smaller, contained region on the molecule of a hormone.  That said, additional scientific research conducted on animal test subjects has demonstrated a theoretical instance of slowing the process of aging; the caveat to this finding is that in the case studies, the peptide is applied on a regular basis.  This theoretical slowing of the aging process is thought to have connections to Fragment 176-191’s ability to burn adipose tissue on a more efficient basis.

Fragment 176-191’s Functional Nature

Fragment 176-191’s functionality is chiefly related to two parts of an animal test subjects’ cell:

• The cytoplasm – the water-like part of the cell that contains all of a cell’s organelles.
• The endoplasmic reticulum membrane – the cell organelle responsible for protein transport and synthesis.

In a natural setting, Fragment 176-191 stimulates the ubiquitin-protein hydrolase involved in processing ubiquitinated proteins and ubiquitin antecedents.  This enzyme will then mark the peptide bond at the glycine C-terminal of ubiquitin.  It may also bond to a free monobiquitin in order to halt the degradation of lysosomes; the cell organelle responsible for breaking down waste materials and other cellular debris.  Fragment 176-191 spreads through the body via the neuroendocrine system.

Positive Results

Scientific research based on animal test subjects has yielded positive results regarding the use of Fragment 176-191.  Firstly, the peptide’s unique structure allows it to fuel lipolysis at a rate 12.5 times stronger than an animal test subject’s natural hormone, thus leading to more efficient fat burning.  Secondly, most of the negative side effects associated with other hormone applications to animal test subjects have not been present with Fragment 176-191.

Insulin’s Relation to Fragment 176-191

Scientific studies on animal test subjects have also led to an interest in studying Fragment 176-191’s effect relating to insulin.  These studies have determined that the peptide increased blood glucose level in animal test subjects over a short period of time.  What’s more, they were able to attain a longer lasting increase in insulin levels in the subjects’ plasma.  These findings enabled researchers to demonstrate how amino acids operate in concert to improve the regulation of insulin travel as a means of achieving homeostasis.  Furthermore, these studies show that bioactive peptides like Fragment 176-191 can remain functional with a minimum of the proper informational sequence.

For Scientific Research Purposes Only

Although there have been several positive aspects that have been connected to the scientific study being conducted with Fragment 176-191, it still must be noted that such application is still in the research phase of things, meaning that its effects are still very much being tested.  What’s more, the results stemming from the peptide’s application, while they have been positive in nature, have only stemmed from research conducted through laboratory tests, and have not been confirmed outside of a lab setting.  As a result, all positive results that are taken from testing Fragment 176-191 must be viewed as a product of scientific research on animal test subjects and nothing more than that for the time being.

 

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PT-141 is a research cyclic peptide that is being examined for its potential positive effects relating to hemorrhagic shock and reperfusion industry.  It commonly goes by the name Bremelanotide.

PT-141’s Functionality

PT-141 is designed to stimulate the melanocortin receptors MC3-R and MC4-R in the central nervous system of animal test subjects.  The receptors that PT-141 targets work to block and regulate specific signals which are transmitted from the brain to the components of the central nervous system relating to negative body functions like inflammation or blood flow restriction.  This type of receptor activation results in a modulation of inflammation and a limiting of ischemia, also known as a restriction in blood supply due to factors related to blood vessels.  As such, the functionality of PT-141 through as derived through scientific studies is to limit bodily irritation caused by various pathogens, as well as to curb damage or dysfunction of blood vessels and associated tissues.  Because the peptide acts through the central nervous system, it does not express itself directly via the bloodstream.

PT-141’s Origins

Previous scientific studies determined that PT-141 induced lordosis amongst animal test subjects; a sexual response that in essence is defined by an animal’s willingness and desire to mate.  It is also marked by aiding in the copulation of animals through physical characteristics involving an animal’s hips and back.

These scientific findings amongst animal test subjects were eventually balanced out by the discoveries of negative side effects in regards to maintaining a state of lordosis for an extended period of time.  Specifically, the peptide was linked to increases in blood pressures as well as various negative gastronomical events.  Today, scientific study is still using animal test subjects in order to test the peptide’s connection with male and female dysfunction, including the activation of lessening sexual drive.

Other Current Scientific Study

Currently, scientific study in regards to PT-141 is focused on managing hemorrhagic shock and reperfusion injury.

Hemorrhagic shock is a potentially serious condition marked by decreased tissue perfusion, resulting in the inadequate delivery the oxygen and nutrients essential for proper cellular function.

There are four classes of cellular shock.  They are:

• Neurogenic
• Cardiogenic
• Hypovolemic
• Vasogenic (also referred to as septic)

These classifications of shock can result in several potentially dangerous scenarios in animal test subjects, including serious issues tied to the cardiovascular system like decreased cardiac output and decreased pulse pressure.  PT-141 theoretically aids in the stimulation of neural reflexes for purposes of elevating sympathetic outflow to the heart and other organs that may otherwise significantly slow or cease operation as a result of hemorrhagic shock.  This stimulation includes factors like elevated heart rate, vascoconstriction, and a redistribution of blood flow away from organs that a body would view as non-vital, such as kidneys or skin.

Reperfusion injury refers to tissue damage caused by the blood supply reentering into the tissue after an ischemic episode like a stroke.  The lack of nutrients and oxygen from blood during an ischemic period generates a condition where the restoration of circulation results in oxidative damage and inflammation through oxidative stress as opposed to the restoration of proper functionality.

This type of injury plays a rather significant role in the brain’s ischemic cascade, which is the series of biochemicial reactions that start in the brain and other aerobic tissues seconds or even minutes after an ischemic episode is detected.  These reactions can lead to strokes, cardiac arrest, and other traumatic injuries.  Additionally, reperfusion injury can manifest in other forms of brain failure, such as the moments following the reversal of cardiac arrest.  If forms of reperfusion injury occur on a multiple basis, other ailments such as the formation of chronic wounds could occur.  Furthermore, the healing of such wounds could also be slowed down.  PT-141 works neurologically to lower the inhibitions associated with blood flow restriction to tissues as a result of the ischemic cascade.  This would hypothetically lessen or even halt the resultant damage that could come as a result from a limitation of blood flow in the areas that would be potentially affected.

Scientific Research

It should be noted that PT-141 is still being in the scientific research phase, and that all of its documented findings in relation to its mechanics, functionality, benefits, and side effects have been culled from studies done within the confines of a controlled environment.  As such, the peptide should only be used and studied within an strict environment that is solely meant for further research, such as a laboratory or medical research facility.

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Triptorelin is a gonadotrophin-releasing hormone (GnRH) agonist.  It is a decapeptide, which means that it consists of a chain of 10 amino acids.  It is used as the acetate of pamoate salts, meaning that it can be used as a counter ion of a compound in order to increase water solubility.

The Functionality of Triptorelin

Triptorelin’s primary functional mechanism is to induce constant stimulation of the pituitary gland; the pea-size gland found in the hypothalamus that is responsible for regulating and controlling several key functions related to an animal test subject’s endocrine system.  Some of the functions the pituitary gland regulates include:

• Growth regulation
• Blood pressure regulation
• Thyroid gland function
• Metabolism
• Temperature regulation
• Pain relief

Scientific research conducted on animal test subjects have determined that as Triptorelin stimulates the pituitary gland, it decreases the subjects’ production of luteinizing hormone.  This is the hormone that regulates and controls the production of estrogen in female animal subjects and testosterone in male animal subjects.   It also plays a key role in the regulation and control of the reproductive process.  Triptorelin also decreases the production of follicle-stimulating hormone.  This is the hormone that controls and regulates the development, growth, and pubertal maturation within animal test subjects.  It also plays a key role in the regulation of the reproductive process.

Theoretical Benefits of Triptorelin

Because Triptorelin’s functionality has been linked to inhibiting the release of certain hormones within animal test subjects, scientific research has yielded a host of theoretical benefits that can be linked to the use of the peptide.  Some of these theoretical benefits include:

• Treatment of hormone-responsive cancers.  Certain forms of cancers, most notably prostate cancer and breast cancer, have been partially linked to the secretion of luteinizing hormones; specifically, these hormones’ association with estrogen and testosterone levels.  Because Triptorelin’s capability of inhibiting the production of luteinizing hormones, scientific study has theorized that the peptide could be used to stem or slow the effects of the cancers that have been linked to the secretion of the hormone.
• Treatment of precocious puberty.  Scientific study based on animal test subjects has led to the theory that the use of Triptorelin could slow the process of puberty occurring at an unusually early age.  The reason for this theory is due to the peptide’s ability to inhibit the release of follicle-stimulating hormone, which regulates the development and pubertal maturation of animal test subjects.
• Treatment of estrogen-dependent conditions – Triptorelin’s ability to inhibit the production of luteinizing hormone means that it also has the ability to slow the production of estrogen in female animal test subjects.  This has led to the scientific theory that certain estrogen-dependent ailments can be treated through the peptide’s usage.  One of these conditions is endometriosis; the gynecological condition where cells from the uterus lining appear and thrive outside of the uterine cavity, causing pain and infertility.  Another condition is uterine fibroid; a benign tumor originating from smooth muscle tissue that could cluster within the uterus and are associated with painful menstruation as well as painful sexual intercourse.

Possible Side Effects of Triptorelin

Scientific study based on animal test subjects has determined that there are several negative side effects that have been theoretically linked to Triptorelin.  Some of the more common negative side effects include:

• Fever
• Decrease of testicle size in male animal test subjects
• Joint pain
• General discomfort
• Diarrhea
• Muscle Pain
• Insomnia
• Shivering

Conversely, some of the more common side effects that have been theoretically linked to Triptorelin include:

• Pain in bladder
• Swelling or bloating in face or extremities
• Bloody or cloudy urine
• Blurry vision
• Decrease in urination frequency or urination volume
• Difficulty breathing

Scientific study based on animal test subjects have also led to the theory that the use of Treptorelin could result in more serious negative side effects, including problems relating to high blood pressure or heart disease.

For Scientific Use Only

While scientific study has been conducted on animal test subjects to determine the functionality and operational mechanics of Treptorelin, as well as its theoretical benefits, and theoretical negative side effects, it should be noted that any and all findings that are associated to the peptide is still solely derived from animal test subject study.  Because it is currently in the research phase, any research relating to Treptorelin should solely be contained to the restrictions of a strictly controlled environment such as a laboratory or a clinical research facility.

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Ipamorelin is a secretagogue peptide, meaning that can play a role in energy homeostatis as well as the regulation and control of body weight in animal test subjects.  It is similar to the peptide GHRP-6, with one of the chief differences being that Ipamorelin is a penta-peptide as opposed to a hexa-peptide.  In other words, the peptide consists of five sides instead of six.  It is considered to be an agonist, meaning that it has the capability to bind to certain receptors of a cell and induces a cellular response.  The peptide is administered to animal test subjects via subcutaneous injection as part of ongoing scientific research in relation to studying its operational mechanisms and properties.

The Fuctionality of Ipamorelin

According to scientific research conducted on animal test subjects, the primary function of Iparmorelin is to stimulate the pituitary gland.  This is the pea-sized gland found at the base of the brain that is responsible for regulating an organism’s endocrine-based functionality.  These various functions include:

• Regulation of bodily growth
• Regulation of hyroid gland function
• Regulation of blood pressure
• Pain relief
• Regulation of temperature

Part of Ipamorelin’s functionality is that it stimulates the production of a hormone that is secreted by the pituitary gland of animal test subjects.  At the same time, the Ipamorelin has been shown through scientific research conducted on animal test subjects to inhibit the production of somatostatin; a peptide that is chiefly responsible for blocking the release of some hormones.  Additionally, the peptide has been shown to increase the production of IGF-1.   This hormone, also known as Insulin-Like Growth Factor 1 or somatomedin C, is similar in the molecular build of insulin which is secreted in animal test subjects as an endocrine hormone, which through scientific research as determined to be the chief anabolic mechanism of action for some hormones.  This portion of the peptide’s functionality makes it similar to the operational tendencies of GHRP-6.  However, unlike the GHRP-6, Ipamorelin works to bind to major control points of appetite, gastric, and growth motility.  In other words, scientific research on animal test subjects have determined that the peptide does not induce an increase in hunger levels, which has been determined to be an effect found in GHRP-6.

Scientific studies on animal test subjects also show that Ipamorelin does not significantly increase the production levels of cortisol; the hormone found in animal test subjects that increases blood sugar through the process of gluconeogenesis.  It also does not significantly increase the production levels of prolactin; the hormone that is plays an important role in regulating the immune system of animal test subjects, primarily as it relates to the process of lactation.

Benefits of Ipamorelin

Scientific research that has been conducted on animal test subjects has determined several different theoretical benefits that have been linked to Ipamorelin.  These theoretical benefits include:

• Increased fat loss
• Rejuvenation of joints
• Strengthening of joints
• Strengthening of connective tissue
• Strengthening of bone mass
• Improved skin tone

These types of positive benefits have led some scientific studies to determine that the peptide could carry several theoretical benefits as they relate to the slowing down of the aging process.

Side Effects of Ipamorelin

The negative side effects of Ipamorelin, according to scientific research that has been conducted on animal test subjects, are determined to be minimal.  These negative side effects primarily have been known to consist of headaches and head rushes (also referred to as a feeling of light-headedness).  The research that has been conducted on animal test subjects has determined that these side effects are relatively mild in nature.  Furthermore, the list of negative side effects has been determined to be significantly shorter than the list of side effects that are typically associated with the peptide GHRP-6.

For Clinical Research Only

While scientific study conducted on animal test subjects have determined a basic outline relating to the operational mechanisms and functionality of Ipamorelin, it should be noted that work with the peptide is still currently confined to the research stage.  Any positive benefits or negative side effects that have been documented through scientific research on animal test subjects is still a product of research that is still ongoing and not conclusive.  Therefore, it is crucial to note that any observation or findings regarding Ipamorelin in relation to its overall mechanisms, operational properties, positive benefits, or negative side effects should be contained to the confines of a strictly controlled environment such as a laboratory or a research facility.

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CJC-1295 is a 30-amino acid peptide that has the ability to bioconjugate within the globular protein serum albumin.  In other words, it has the capability to join a pair of bimolecules together via a chemical bond.

How CJC-1295 Works

The component that allows CJC-1295 to function as it does is found within the peptide chain GHRH1-29.  The discharge of the peptide is related to the negative feedback loop that is part of the growth hormone axis found in animal test subjects; this axis regulates the production of the animal’s growth hormone for homeostatic purposes.  The issue with this component is its rapid half-life, which lasts fewer than seven minutes.  However, studies on animal test subjects have shown that CJC-1295 boosts the half-life of GHRH1-29, as well as its bioavailability.  This in turn enables GHRH-1 to have an extended effect on animal test subjects.  According to scientific study, this boost has been dramatic, as it has been shown to extend the half-life to over seven days.

In addition to creating a more stable peptide, CJC-1295 enhances bioactivity, blocks methionine oxidation, and decreases asparagines rearrangement or amide hydrolysis to asparatic acid.  These mechanics essentially cause the growth hormone axis in animal test subjects to stay active in for a significantly longer time.

Bioconjugation

CJC-1295’s capacity to extend GHRH1-29’s half-life is linked to the relatively new technology of bioconjugation.  This process can take a reactive group and attach it to a peptide, which in turn reacts with a nucleophilic unit found in an animal test subject’s bloodstream to form a bond that is more stable.  This peptide has a high binding affinity for albumin, and this affinity blocks natural degradation, which causes an extension of the peptide’s half-life and bioavailablity.

Benefits of CJC-1295

Scientific studies on animal test subjects have led researchers to believe that CJC-1295 could have the following benefits:

• The boosting of protein synthesis.  CJC-1295 is thought to increase the amount of proteins that an animal test subject can generate by blocking natural cellular degradation.
• Reduction of body fat –CJC-1295’s mechanics have been shown to promote lipolysis, otherwise known as the process where lipids get broken down.  This degradation of lipids, in turn, makes body fat to decrease.
• Improved deep sleep – Scientific studies on animal test subjects have determined that CJC-1295 has enabled the subjects to maintain a deep sleep on a more consistent basis.  Studies theorize that this kind of behavior is linked with the peptide’s abilities to promote muscle growth and memory retention. These studies also show that this particular benefit tends to dissipate over time.
• Growth of muscle tissue.  The increase of proteins translates into a boost in muscle cells.  This has led to an amplification in the mass and size of muscles found within animal test subjects.
• Increased bone density – Scientific studies performed on animal test subjects have determined that CJC-1295’s usage over a specified amount of time can cause the generation of a bone’s mineral matter per square centimeter to boost.  This enhanced process enables bones to be stronger and less vulnerable to fractures and other bone-related injuries.
•  Expedited injury recovery – The boost in protein production translates to a more efficient healing process within animal test subjects.
• Stronger immune system – Increased protein production has also been shown to improve animal test subjects’ capability to fight off sickness more efficiently.

It should be noted that even though positive determinations are being chronicled, these perceived benefits are still being verified for purposes of consistency.

Potential Side Effects

While scientific research on animal test subjects has led to the determination of several positive benefits in relation to CJC-1295, there are also a few negative side effects that have been recorded.  These side effects include:

• Retention of water
• Fatigue
• Temporary numbness of extremities

Studies have thus far determined that the recorded cases of negative side effects are far less than the positive effects that have been marked.  Additionally, some of these studies have determined that the negative side effects tend to skew toward being inherently mild.

It should be noted that, much like the positive benefits, the negative side effects are still being verified through scientific study to determine their consistent manifestation.

It should also be noted that because the benefits, effects, and overall mechanics and functionality relating to CJC-1295 are still being determined, the use of the peptide is still contained to laboratories.  Therefore, it is not fit for use outside of a controlled research environment, where it can be used for scientific research on animal test subjects.

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GHRP-2 is a secretagogue whose chemical makeup enables it to promote the natural secretion of growth hormone amongst animal test subjects, per scientific research.  At the same time, the peptide can stimulate the pituitary gland, the pea-sized gland found in the brain that is regarded as the heart of the endocrine system.

How GHRP-2 Works

GHRP-2’s main function as determined by scientific research conducted on animal test subjects is centered on building up muscle mass and stimulating hunger.

The peptide can accomplish both of these elements because it stimulates the inner workings of the pituitary gland, which causes an increase in the synthesis of proteins in animal test subjects.  It can achieve this because it can prevent somatostatin; a peptide hormone that controls the endocrine system and influences cell propagation and neurotransmission via interaction with G protein-coupled receptors.  Additionally, scientific studies have found that GHRP-2 can raise the levels of calcium ion influx, which can promote more growth production in animal test subjects.

GHRP-2 also stimulates the production of ghrelin; a self-regulating peptide produced chiefly by the stomach as a means to stimulate hunger in animal test subjects.  This enhanced ghrelin production allows for an increased desire amongst animal test subjects to eat.  Furthermore, GHRP-2 also promotes eleveated levels of IGF-1; a protein produced by the liver that plays a large role in muscle and tissue repair and growth.

Additionally, GHRP-2 has been connected to an increase in hypothalamus functionality.  This boost, like the increase in ghrelin production levels, also helps to increase appetite in animal test subjects.

GHRP-2 does have a markedly low half-life, ranging from 15 minutes to an hour once it has been given to an animal test subject.  This means that the peptide’s effectiveness is very limited in animal test subjects unless it is given to them frequently.

GHRP – 2 Benefits

According to scientific research conducted on animal test subjects, GHRP-2 has been determined to contain host of theoretical benefits.

The primary theoretical benefit based on animal test subject research is the promotion of muscular repair and growth.  This is due to the peptide’s capability to induce a higher level of protein secretion relating to growth and repair.

The secondary theoretical benefit is an increased appetite.  Because GHRP-2 promotes the production of ghrelin, animal test subjects experienced an increased tendency to feel hungry.  This increase is coupled with the peptide’s ability to break down fat mass.  GHRP-2’s mechanics enable animal test subjects to burn off adispose tissue at a faster rate, leading to the subject’s ability to break down excess fat cells more efficiently.  This in turn allows for the fat of animal test subjects to be diminished over a shorter time frame, as well as an increased maintenance of incoming fat cells.

A third theoretical benefit of the peptide it its possible capability to improve the anti-inflammatory actions in an animal test subject.  Scientific research has determined that GHRP-2 can potentially lessen instances of negative reaction that an animal test subject’s body may have to damaged cells, irritants, or other assorted pathogens.  These reactions include swelling, pain, decreased functionality, and more.

Other theoretical benefits concerning GHRP-2 include:

• Enhanced defense of the liver
• Improved skin elasticity
• Improved bone density
• Lowering of cholesterol levels

GHRP-2’s Side Effects

While scientific research on GHRP-2 conducted via animal test subjects have resulted in several theoretical benefits, several negative side effects have been noted as well.   The side effects that have been linked to GHRP-2 include:

• Tightness and/or carpel tunnel-type symptoms.
• Tingling and numbness in the extremities.
• A decrease in insulin sensitivity.
• An increase in water retention.
• Increased instances of fatigue.

Notes about Clinical Studies and GHRP-2

While both positive theoretical benefits and negative side effects have been linked to GHRP-2 in conjunction with scientific research on animal test subjects, it should be noted that these types of test results have not been determined to officially be considered consistent.  The reason for this chiefly due to the fact that the inner workings of the pituitary gland have a tendency to respond differently to the peptide from one animal test subject to another.

This, among other reasons, is why it also be noted that GHRP-2 is still in being researched scientifically on animal test subjects.  Because of this, it is considered to be a lyophilized peptide and should only be used for clinical research.  Its processes, operations, and mechanics should only be viewed within the parameters of a strictly and thoroughly controlled environment, such as a scientific research facility or a laboratory.

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A peptide is typically defined as a chain of amino acid monomers (that is, a molecule that may chemically attach to other molecules to form a polymer) which are linked by covalent bonds.  They are typically split into two groups:  Long chain peptides, also known as polypeptides or proteins; and short chain peptides, sometimes referred to as ogliopeptides.

Peptides play a large role within a certain subset of biomimetic materials, which are substances developed using elements that naturally occur in nature.  The particular subset of biomimetic materials that pertains to peptides relates to tissue engineering; the process in which cells, materials, and engineering is combined with appropriate biochemical and physio-chemical aspects to enhance, repair, or replace biological functions of tissues found in living organisms (M. Radisic, et al, 1357-1368).

The primary use of peptides in tissue engineering results from their ability to elicit responses by mimicking extracellular matrix, or ECM, proteins.  In essence, by replicating the functionality of these proteins, peptides can manipulate various biological functions, outside the realm of the normal physiological regulations, as dictated by an organism’s typical processes.  (Shin, H, et al, 4353-5364)

While both forms of peptides share some similar traits that make them essential study components, other aspects of their behavior are unique. (Shin, H, et al, 4353-5364)

The Functionality of Long Chain Peptides

A long chain peptide is referred to as a polypeptide because it is a lengthy, continual chain of polymers made up of many amino acids – typically between 10 and 100 –linked together chemically.  Long chain peptides have a molecular weight of up to about 10,000 grams per mole, and can fold into specific three-dimensional configurations.  These types of peptides are commonly referred to as proteins.  They are largely considered to be the core components of basic biological processes found within living organisms.  Some of the functions that proteins perform include:

• DNA replication – The process of making two identical copies out of one original DNA molecule.  It is the foundation for biological inheritance for all living organisms.  In essence, this is the code that determines an organism’s physical makeup.
• Cell signaling – The complex system of communication that controls and regulates essential cellular activities and coordinates a cell’s action.  This sometimes falls under the parameters of responding to stimuli.  This communication is responsible for maintaining an organism’s overall systematic functionality.
• Enzyme catalysis – The process of controlling the rate of a chemical reaction by specialized proteins as a means to maintain biological efficiency. (G. Chaturvedi, 1-7)

Polypeptides regulate or trigger a significant amount of organic functions, either acting near to or distance from the site where they are produced and released.  Their manner of regulation can be traced back to the hormones that they help to express within the organism.  These hormones help to regulate various essential functions that enable an organism to operate normally, from antidiuretic (that is, water retaining) action in the kidneys to blood sugar control in the pancreas.  (G. Chaturvedi, 1-7)

Because of their lengthy size, long chain peptides have higher instability than their short chain counterparts.  While a polypeptide contains a wealth of information within its construct, its physical structure allows for more potential manifestations of degradation through processes such as:

• Hydrolysis – The process in which chemical bonds experience cleavage, otherwise known as division, due to the addition of water.
• Racemiztion – The process in which a conversion of an enatiomerically pure mixture (that is, where only one enantiomer is present) into some sort of mixture where more than one enantiomers are present.  (G. Chaturvedi, 1-7)

Polypeptides can also experience issues pertaining to physical degradation depending upon their molecular weight, such as:

• Denaturation –The process in which proteins or nucleic acids lose the structure that is present in their native state due to external stress, resulting in the disruption of cell activity or even cell death.  Some of these external stresses include a concentrated inorganic salt, a strong base, a strong acid, heat, or an organic solvent such as alcohol.
• Self Association – The process in which a long chain peptide interacts selectively and in a non-covalent way within itself.
• Gelation – The process where a fluid solution is converted into a semi-solid mass composed of multiple peptide fibrils and tangled within a complex mesh.
• Adsoprtion – The process in which atoms or ions form a gas, liquid, or a dissolved solid to adhere to a molecule’s surface.  This process is a consequence of surface energy, which disrupts intermolecular bonds.  This process is sometimes marked with the polypeptide collapsing.
• Aggregation – The process in which a protein structure creates its shape is known as protein folding.  Occasionally, these proteins get mis-folded, which inhibits their proper functionality.  The process of aggregation relates to the erroneous process  that occurs when misfolded proteins accumulate at either an intracellular level or an extracellular level.  (G. Chaturvedi, 1-7)

This high level of chemical instability makes the study of polypeptides a difficult challenge, as numerous paths of disruption makes it difficult to obtain and determine proper and consistent clinical results.

The Functionality of Short Chain Peptides

By contrast, short chain peptides (which are sometimes known as oligopeptides) are significantly smaller chains of amino acids.  These amino acids are sequentially bonded together to form peptide bonds.  These short peptide chains do not contain proteins.  While there is no definitive maximum number of amino acids a chain can include and still be considered a short chain peptide, the minimum number of amino acids that must be present to be considered a short chain peptide is only two.  (Scitable)

Short chain peptides, however, can share similar traits with long chain peptides or polypeptides.  For example, they both can secrete hormones, which are essential components for the overall mechanics and operations of an organism (Scitable).  However, short chain peptides do have an advantage over long chain peptides in that the smaller chain size is more stable.  Small chain peptides do not experience some of the issues that long chain peptides do because of their shorter length—most notably collapsing during absorption.  Additionally, short chain peptides can be replicated much more efficiently (Shin, H, et al, 4353-5364).  This makes them significantly more attractive for research.  The stability and efficiency of short chain peptides results in a more stable base of research metrics from which a valid library of case studies can be created.  Because short chain peptides won’t collapse as a result of their length, research done with short chain peptides provide more consistent, stable data and results.  This, in turn, provides researchers with more accurate, definitive set of data overall. (Shin, H, et al, 4353-5364)

Peptides and Tissue Engineering

The primary focus of short chain peptide research on tissue engineering is to discover and develop biocompatible materials to help combat natural degradation that is part of the aging process.

Specificallyamino acids located within the peptides are used as building blocks by other biological.  These peptides are often referred to as “self-assembling peptides,” because they can be modified to contain biologically active motifs (Holmes, 1).  This enables them to replicate information derived from tissue and to reproduce the same information independently.  Thus, these peptides act as building blocks capable of conducting multiple biochemical activities—up to and including tissue engineering.

It should be noted that tissue engineering research currently being performed on both short chain and long chain peptides is still in early stages.  As such, any research data or metrics relative to the peptides’ effects on tissue engineering should only be considered as preliminary.

Sources

Radisic, Milica; Park, Hyoungshin; Grecht, Sharon; Cannizzaro, Christopher; Langer, R.; Vunjak-Novkovic, Gordana; “Biometric Approach to Cardiac Tissue Engineering,” Philosophical Transactions:  Biological Sciences Vol. 362, No. 1484, Bioengineering the Heart (August 29, 2007; pg. 1357-1368)

Shin, H; S. Jo, and A.G. Mikos; “Biomemetic Materials for Tissue Engineering,” Biomaterials, 2003.24; p. 4353-5364

Chaturvedi, Gunja; “A Report on Stability of Polypeptides and Proteins,” Birla Institute of Technology and Science, Pilani (Rajasthan), August 2009, p. 1-7

Kyle, Stuart; Aggeli, Amalia; Ingham, Eileen; McPherson, Michael J; “Recombinant Self-Assembling Peptides as Biomaterials for Tissue Engineering”; Biomaterials, 31(36); December 2010, p. 9395-9405

Scitable, “Peptide Definition”, www.nature.com/scitable/definition/peptide-317

Holmes, Todd C.  “Novel peptide-based biomaterial scaffolds for tissue engineering; Trends in Biotechnology, Vol. 20 No. 1 January 2002

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GHRP-6 is a secretagogue peptide used to increase the amount of natural secretion growth hormone in the body of animal test subjects.  It is a hexipeptide; that is, it contains special chain made up of six amino acids.

GHRP-6’s Functionality

GHRP-6 has been determined through scientific research to cause an increase in stimulation of the pituitary gland in animal test subjects.  This tiny gland located at the brain’s base is chiefly responsible for regulating several important bodily processes including:

• Water regulation
• Thyroid gland functionality
• Growth
• Pain relief
• Blood pressure
• Temperature regulation

GHRP-6’s presence inhibits the gland’s capability to block hormone productions in an animal test subject, which in turn results in an enhanced ability to produce hormones related to an animal test subject’s growth.  Additionally, the peptide impacts an animal test subject’s central nervous system, as it assists in the activation of intracellular signaling pathways used by hormones as it elevates the process of cell survival.  This correlation between the central nervous system and the peptide has led researchers to theorize that it could have a significant effect of guarding cell loss and function during hypoxic-ischemic brain injuries such as a stroke.

A second component to GHRP-6’s functionality is how it works with ghrelin; the amino acid primarily produced by the stomach as a means to stimulate hunger.  The peptide increases the production of ghrelin, which enables animal test subjects to feel hungry longer.  This then elevates the need for a higher intake of food, and this intake provides more fuel which can then be converted into the hormones secreted by the pituitary gland in animal test subjects.

What’s more, GHRP-6 leads to an elevated secretion of IGF-1.  According to scientific research, this natural secretion is determined to be the primary anabolic mechanism for the hormone that promotes growth in animal test subjects.  These studies show that GHRP-6 promotes a higher release of IGF-1 through the animal test subjects’ central nervous system.

GHRP-6’s Theoretical Benefits

Currently, GHRP-6 is being scientifically studied on animal test subjects.  These studies have led to the theory that the peptide could have several theoretical benefits, including:

 

• Muscle growth increase – GHRP-6’s chief mechanism allows it to promote the increase in secretion of the hormone that causes growth in animal test subjects, which in turn aid and promote the further development of muscle mass.  These hormones can also speed up the process of muscle and tissue repair.
• Body fat decrease – Although GHRP-6 elevates the production of ghrelin and increases hunger, the peptide’s capability to allow the liver to secrete an elevated level of IGF-1 enables energy to burn faster in animal test subjects.  This results in the subjects’ bodies being able to break down fat tissue more efficiently.  This process has also led to a theory that an animal test subject could experience weight gain if the increased food is not converted to energy.
• Bone tissue growth increase – GHRP-6’s promotion in hormone secretion also aids in creating an increased bone density amongst animal test subjects.
• Increased Immune System Efficiency – GHRP-6’s ability to stimulate the pituitary gland allows for animal test subjects to heal from injury and illness more efficiently.  This process ties into the pituitary gland’s ability to promote pain and injury recovery through the body.
• Connective tissue and joint strengthening – Because GHRP-6’s mechanics promote growth hormone production in animal test subjects, studies have theorized that joints and connective tissue could be repaired quicker.

GHRP-6’s Theoretical Side Effects

Even though scientific research through animal test subjects have determined several theoretical benefits linked to GHRP’6, several case studies have also determined that the peptide does theoretically have some negative side effects.  Among these negative theoretical side effects are:

• Light-headedness
• Increase in hunger
• Dizziness
• Nausea
• Soreness of bones
• Tingling or numbness on the skin
• Reduction of touch sensitivity

In addition, some scientific research conducted on animal test subjects have led to the theory that GHRP-6 could cause hypoglycemia.  However, there have not be conclusive enough studies or anecdotal evidence on record that hold up these particular theories.

For Case Study Only

As of right now, GHRP-6 is still locked in the scientific study phase.  All findings, reports, and theories in relation to the peptide’s operation, mechanics, theorized benefits, or speculated side effects have been culled from scientific research conducted on animal test subjects.  Any surveillance related to GHRP-6 and its mechanics and processes should be contained to a strictly controlled and regulated environment, such as a laboratory or a research facility.

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The clinical study of peptides has been long been considered to be important and crucial research (Fields, et al).  Gaining a complete understanding of the operational mechanics of peptides could lead to a wide range of important scientific discoveries.  One of the most vital areas of investigation is how peptides can potentially inhibit cancer proteins.  (Thundimadathil, J.)

The Functionality of Peptides and Cancer

Peptides are short chains of amino acid monomer molecules linked through a covalent chemical bond (Scitable).  They are designed to start, promote, and prohibit several cellular functions through chemical secretion—from paracrine and endocrine signals to various growth factors and neurotransmitters.  Operating at the cellular level, peptides secrete elements that promote and regulate a wide variety of cellular systems.  (Peptide Guide).

Like peptides, cancer’s origins are also cellular based.  It is a disease characterized by uncontrolled cellular division.  Production of excess cells have the ability to invade other cellular tissues.  This invasion results in the formation of a tumor. If this tumorous mass is left to grow, it develops vascularization (the formation of blood vessels) and eventually metastasis (spreading of the disease throughout the organism).  These latter two steps play a major role in transitioning a tumor from a benign into a malignant state.  When a tumor reaches malignancy, it can cause serious issues, including death of the organism.

Clinical research has studied the nature of peptides to determine the role that they can play in preventing the cancer from initializing, as well as combating the cancer in the event that it establishes itself inside of the organism and starts to metastatize (Thundimadathil, J.).

Peptides as an Effective Ally

There are several reasons why science is turning to peptides in the search for the control and eradication of cancer, including:

• Size – Because peptides are molecular in nature, can infiltrate and interact with the cancer-causing agents at the cellular level.
• Ease of synthesis and modification – The nature of peptides is such that they can easily replicate and change behavioral patterns at a cellular level by affecting basic regulatory procedures such as inhibiting or promoting secretions.
• Tumor penetration – Clinical studies of animal test subjects have determined that peptides can infiltrate tumors extremely efficiently, giving them the ability to potentially disrupt cellular production within the tumor after its formation.  This would lessen the risk of a tumor transforming from benign to that of a malignant state.
• Excellent biocompatibility – The term biocompatibility refers to the ability of a material or substance to perform with an appropriate host response in a specific situation.  The term describes how well a peptide interacts with a host subject.  Clinical studies on animal test subjects have shown that peptides do interact efficiently with cancer cells. (Thayer, pg. 13-20)

These attributes indicate that peptides represent a potentially promising therapeutic agent in the fight against cancer.  (Thundimadathil, J)

Major Peptide Applications against Cancer

Clinical research on animal test subjects, exploring the complex interactions between peptides and cancer-causing agents, has suggested several different avenues in which peptides may be applied to various cancer scenarios. (Thundimadathil, J)

The most promising application is through peptides that target LHRH (Miller, er al; 231-233).  These particular peptides act as an agonist, meaning that they bind to a cell in a way that regulates LHRH receptors.  The process of inhibiting the cell receptors suggests that peptides could be beneficial in fighting prostate cancer.

A second application being considered involves peptides as radionuclide carriers (Strowski and Blake, 169-179).  A prevalent amount of neuroendocrine tumors are marked by an aggressive overexpression of somatostatin receptors.  Somatostain is the peptide hormone secreted to regulate the endocrine system.  Their receptors also carry an impact on neurotransmission and cell proliferation; hyperactivity of these receptors may lead to an overabundance in cellular production which may in turn cause tumors to form.  The introduction of a peptide that is a radionuclide, or a radioactive nuclide, can help neutralize these overexpressed receptors.  Clinical studies on animal test subjects have determined that the neutralization has to do with the somatostatin receptors’ inherent makeup.  The somatostatin receptors found in tumor tissues are denser in nature than non-tumor tissues.  This difference in density creates a higher rate of attraction to radionuclide peptides, and therefore is subject to targeting by the peptides more readily than non-tumor tissue.  Because of its link to the endocrine system, there is particular interest in this application to combat cancers produced by the endocrine system.  While this process does have the potential to play a role in the field of nuclear medicine, it should be noted that because of the peptide’s radioactive nature, there are many concerns about this approach.

A third application currently being evaluated is peptide vaccines (Henderson, et al, 2359-2362).  This method of active immunization is derived from the concept of introducing immune cells or molecules into the animal test subject.  The basis for this potential type of cancer treatment depends on vaccines containing peptides derived from a protein sequence of antigens produced by the cells of a corresponding tumor.  These antigens, which are also known as tumor-associated antigens or TAAs, are typically identified as invaders by the animal test subjects’ immune system.  Reintroducing these antigens via a vaccination can potentially induce a systematic immune response by the animal test subject that could result in the destruction of cancers throughout the organism.  On a larger scale, this type of treatment may lead to the regression of a tumor.   While this approach does show potential, its flaw, according to current research, is that the vaccines tend to have a weak immunogenicity—e.g. the peptides do not provoke a strong enough immune response.

A fourth application that is currently being scrutinized via clinical research is using peptides that contain the property of cytotoxicity (Schally and Nagy, pg. 1-14)—the property of being toxic to cells.  These peptides can be designed to form bonds with specific receptors that are known to overexpress the cells that can form tumors, such as somatostatin.  This design enables the peptide to target a cell expressing the desired receptor and therefore kill the resultant cancerous cells.  These particular peptides are sometimes referred to as homing peptides because they are specifically designed to hone in and neutralize or eliminate diseased tissue within the organism..

The final major application that is currently undergoing clinical analysis is the deployment of what are known as anticancer peptides (Rosca, et al, pg. 1101-1116).  These peptideswork by preventing angiogenesis , enzymes, signal transduction pathways, proteins, gene expression, or protein-to-protein interactions from occurring.  These preventions can disrupt the process of tumor growth and neutralize the cancer’s growth.

The Importance of Clinical Research

While various forms of clinical research performed on animal test subjects have determined several potential positive avenues in which peptides may be utilized to treat cancer, it should be noted that there is still a host of research that is left to be done on this subject.  There is still a significant amount of investigation required before the cancer-battling attributes exhibited by peptides can be considered definitive.  Nonetheless, results that clinical studies have produced are encouraging, as these methodologies advance into the future.

Sources

Fields, Gregg B; Alberico, F.; Wade, J.D.; “International Journal of Peptide Research and Theraputics”

Scitable, “Peptide Definition”, www.nature.com/scitable/definition/peptide-317

Thundimadathil, Jyothi; “Cancer Treatment Using Peptides:  Current Therapies and Future Prospects”; Journal of Amino Acids, Volume 2012

Peptide Guide, www.peptideguide.com

Thayer, A.M.; “Improving Peptides,” Chemical and Engineering News, Vol. 89, pg. 13-20, 2011

Miller, W.R.; Scott, W.N.; and Morris, R; “Growth of Human Breast Cancer Cells Inhibited by a Lutenizing Hormone-Releasing Hormone Agonist,” Nature, vol. 313, no. 5999; pg. 231-233, 1985

Strowski, M.Z; and Blake; A.D.; “Function and Expression of Somatostatin Receptors of the Endocrine Pancreas;” Molecular and Cellular Endocrinology, vol. 286, no 1-2; pg. 169-179, 2008

R. A. Henderson, S. Mossman, N. Nairn, and M. A. Cheever, “Cancer Vaccines and Immunotherapies: Emerging Perspectives,” Vaccine, vol. 23, pp. 2359–2362, 2005

A. V. Schally and A. Nagy, “Cancer Chemotherapy Based on Targeting of Cytotoxic Peptide Conjugates to their Receptors on Tumors,” European Journal of Endocrinology, vol. 141, no. 1, pp. 1–14, 1999

E. V. Rosca, J. E. Koskimaki, C. G. Rivera, N. B. Pandey, A. P. Tamiz, and A. S. Popel, “Anti-angiogenic Peptides for Cancer Therapeutics,” Current Pharmaceutical Biotechnology, vol. 12, no. 8, pp. 1101–1116, 2011