CJC-1295 Peptide (No DAC)
CJC-1295 is a synthetic peptide derivative of the naturally occurring GHRH hormone and is composed of 29 amino acids.(2) This peptide is also referred to as Modified GRF (1-29) or CJC 1295 without DAC. It is a modified version of the peptide containing four substituted amino groups that are considered to help prevent the peptide’s degradation. CJC without DAC does not have a Drug Affinity Complex that is sometimes added to further extend the half-life of the peptide. Modified growth hormone fragments GRF (1-29) were first discovered in the early 1980s, when it was suggested that the first 29 amino acids of the natural growth hormone-releasing hormone might retain all the properties of the full 44 amino acid peptide.(3) One of the potential drawbacks of synthetically developed growth hormone-releasing peptides is a short half-life. Rigorous research has resulted in a supposedly stabilized, longer-lasting CJC-1295 (No DAC) peptide.(1)Overview
CJC-1295 without DAC, alternatively known as the tetra-substituted GRF (1-29), represents a synthetic variant of the naturally occurring hormone responsible for the release of growth hormone (GHRH). Scholars have posited that it facilitates the secretion of growth hormone (GH). This compound is essentially constructed from the minimal sequence of amino acids that might bind to GHRH receptors, specifically the initial 29 amino acids of GHRH. There are notable structural differences between CJC-1295 without DAC and the unmodified fragment, primarily due to the alteration of four amino acids within the original 29 amino acids of GHRH. These changes encompass the 2nd, 8th, 15th, and 27th amino acids, and such adjustments might arguably extend the peptide’s lifespan against enzymatic breakdown, particularly by enzymes like dipeptidyl peptidase-4 (DPP-4).(4) More specifically, these alterations include:- The replacement of L-alanine with D-alanine at the 2nd position, which is thought to bolster resistance against molecular degradation.
- The substitution of asparagine with glutamine at the 8th position, which could conceivably minimize asparagine reconfiguration and amide hydrolysis.
- The exchange of glycine for alanine at the 15th position, which is speculated to enhance bioactivity.
- The alteration from methionine to leucine at the 27th position, which is suggested to prevent methionine oxidation.




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