Modified GRF 1-29 was originally named tetrasubstituded GRF 1-29, a description for the 29 amino acids in the peptide that were derived from the growth hormone releasing hormone or GHRH. Specifically modified GRF 1-29 is an altered version of the peptide that is developed from the shortest portion of growth hormone releasing hormone that is fully functional. This is known in scientific circles as growth hormone releasing factor 1-29 which is abbreviated to GRF for the sake of simplicity. This hormone is also sold under the name sermorelin.
This peptide was developed as a way to control growth hormone in the body of animals. Growth hormone can have a variety of effects on the body of the test subjects which are dependent on the different peptides that it comes into contact with as it is released.
Creating synthetic peptides can allow scientists to get a better feel for how these hormones work and the effects that they can develop by encouraging growth hormone to interact with different chemicals in animals. Modified GRF 1-29 works by increasing the production of growth hormone by binding to the receptor cells of the anterior pituitary to encourage this development.
Basics of the Peptide
Modified GRF 1-29 is developed to mimic the structure and effects of growth hormone releasing hormone but it has been slightly altered to encourage stability when it is applied to animal tissue or encouraged to move through the blood stream of an animal test subject.
- The biology of the modified GRF 1-29 chemical structure was based on the 44 GHRH amino acid chains that are biologically active in animal tissue.
- The issue with this peptide is that the natural version that is developed by the body has a half-life which is less than 10 minutes and can drop as low as 5 minutes in most conditions.
The very low half-life of natural versions of GHRH make it difficult for products that are designed to mimic the function of this chemical to sustain a shelf life or interact with chemicals in a measurable way during research, which has caused problems for researchers.
In order to combat the problems associated with the short half-life of GHRH, modified GRF 1-29 was altered in its structure so that it can better suit the needs of the researchers that are working with it.
To create this structure the amino acids at the 2, 8, 15 and 27 place were replaced to create higher yields. This has expanded the half-life of the product to up to 30 minutes when it is exposed to an animal’s blood stream, allowing it to create a higher application of growth hormone in test subjects.
Origins of the Modified GHRH Synthesis
Research has focused on the first 29 amino acids on the growth hormone releasing hormone chain because they were found to be just as potent on their own as they are when they are combined with the full 44 amino acid chain that the body produces naturally.
- The fragment that has come to be known as GRF 1-29 has a rapid metabolic clearance which was synthesized to help to enhance biologic activity, increasing the speed that an animal’s body moved through metabolic clearance.
- The forms of GRF 1-29 were largely created by taking amino acids found in the original GHRH chain were substituted with amino acids that had an increased resistance to the enzymatic cleavage that naturally occurs in an animal’s system.
Early forms substituted L-alanine in the second position of the 29 amino acid chain because this chemical could act as an optical isomer. D-alanine has also been used for this purpose.
Substituting these chemicals creates a peptide bond at the third amino acid in the aspartic acid structure between D-alanine and the other chemicals which helped to increase the cleavage from dipepitdyl peptidase-4 amino acids which in previous experiments has caused the peptide fragment to be inactive.
The first tetrasubstitued GRF 1-29 was studied in detail in 2005 in a study of peptide structured. The term in this writing was basically used to describe a chain that had been used to make the substitutions mentioned above. By 2008 researchers at DatBtrue coined the term modified \GRF 1-29 to describe the peptide structure that is discussed publically today.