GHRP-6 Blend

Research indicates that peptides CJC-1295 and GHRP-6 may exert potential action on growth hormone release. When presented as a blend, they may possibly induce synergistic action, stimulating an organism’s synthesis and secretion of growth hormones. This peptide blend may possibly help repair mild injuries associated with muscles and surrounding ligaments. GHRP-6 Blend

GHRP-6 Blend

GHRP-6 peptide is a synthetic six amino acid peptide analog of ghrelin, a naturally occurring peptide that is considered by scientists to stimulate the secretion of growth hormones and help maintain their concentrations. To do so, researchers hypothesize that it may activate what is known as the growth hormone secretagogue receptor (GHS-R1a). GHRP-6 Blend

In terms of structure, GHRP-6 does not appear to share any homology with ghrelin despite its affinity to the receptors, but instead it appears to be an opioid analog of the peptide Met-enkephalin. Yet, researchers suggest it lacks the opioid activity which is typically associated with these enkephalins. Thus, GHRP-6 is a synthetic hexapeptide that researchers have classified in the group of growth hormone secretagogues (GHSs).

CJC-1295, also referred to as tetra-substituted GRF (1-29), is a synthetic peptide analog of the naturally occurring growth hormone-releasing hormone (GHRH), which is believed by researchers to trigger the release of growth hormones. It is essentially equivalent to the shortest chain of amino acids that may potentially attach to the GHRH receptors, which are the first 29 amino acids of GHRH. The key structural distinctions between CJC-1295 and GRF (1-29) are found in four altered amino acids of the original 29 amino acids of GHRH. These modifications involve the 2nd, 8th, 15th, and 27th amino acids, and may potentially enhance the peptide’s resistance to degradation by the enzyme dipeptidyl peptidase-4. Specifically, the modifications include:

• The substitution of L-alanine with D-alanine at the 2nd position which is believed to increase resistance to molecular breakdown.
• Replacing asparagine with glutamine at the 8th position which may potentially reduce asparagine rearrangement and amide hydrolysis.
• The replacement of glycine with alanine at the 15th position which is hypothesized to augment bioactivity.
• Changing methionine with leucine at the 27th position which is posited to inhibit methionine oxidation.