CJC-1295 DAC

CJC-1295 DAC Peptide

CJC-1295 DAC is a synthetic analog of growth hormone-releasing hormone (GHRH) that has the potential to enhance plasma levels of growth hormone (GH) and insulin-like growth factor 1 (IGF-1).[1] Drug affinity complex (DAC) is an additive component that is considered to prolong the half-life of CJC-1295. Researchers have created several synthetic modifications of growth hormone-releasing hormone (GHRH), which appear to retain certain selective traits of the hormone while eliminating others. CJC-1295 is one such synthetic analog, comprising the first 29 amino acids of GHRH. This is believed to lend secretagogue characteristics with greater solubility, which may be easier to synthesize in larger volumes.

CJC-1295 DAC shares similarities with other GHRH analogs like Sermorelin, as both are derivatives of the first 29 amino acids of GHRH. CJC-1295 is structurally identical to Modified GRF (1-29). In particular, CJC-1295 DAC and Mod GRF (1-29) exhibit four alterations within their 29 amino acid sequence, specifically at the 2nd, 8th, 15th, and 27th positions. These modifications are hypothesized to enhance the peptides’ resistance to enzymatic breakdown, particularly by dipeptidyl peptidase-4 (DPP-4). For instance, the replacement of L-alanine with D-alanine at the 2nd position may contribute to increased resistance to molecular degradation. Substituting asparagine with glutamine at the 8th position may conceivably reduce the likelihood of asparagine rearrangement and amide hydrolysis. The substitution of glycine with alanine at the 15th position is suggested to enhance bioactivity. Finally, the alteration from methionine to leucine at the 27th position is thought to aid in mitigating the risk of methionine oxidation. The primary differential between the two peptides, CJC-1295 DAC and Mod GRF (1-29), is the addition of DAC to the CJC-1295 molecule. DAC is attached to CJC-1295 through a lysine linker to extend the peptide’s pharmacokinetics. DAC appears to facilitate the association of peptides with blood proteins such as albumin. This appears to enhance their half-life, as compared to similar peptides such as GRF (1-29).[2] This occurrence may be attributed to the purported ability of DAC to interact with plasma proteins. Specifically, it seems that the DAC element involves the association of a lysine derivative, N-epsilon-3-maleimidopropionamide, with the C-terminus of CJC-1295 DAC. The incorporation of this altered amino acid sequence into the DAC configuration may plausibly improve the pharmacokinetics of CJC-1295 DAC, potentially prolonging its half-life to around eight days.