Modified GRF (1-29), or Mod GRF (1-29), is a synthetic peptide that is a modified fragment of the endogenously occurring growth hormone-releasing hormone (GHRH). It was first developed in the 1980s when studies indicated that the first 29 amino acids of GHRH may possess all of the biological potential associated with the full-length 44 GHRH molecule.[1]
This discovery led to the development of a truncated version called GRF (1-29), also referred to as Sermorelin by researchers. Mod GRF (1-29) introduces specific modifications to support the peptide’s stability and efficacy. Four amino acids in the sequence are substituted at positions 2, 8, 15, and 27.[2] Here is what some researchers believe about these modifications:
– Position 2: The amino acid alanine is replaced with its mirror image, D-alanine. This substitution aims to increase resistance to enzymatic degradation, thereby improving the peptide’s stability.
– Position 8: Asparagine is substituted with lysine, an amino acid with a positively charged side chain. This change may support the peptide’s binding affinity to GHRH receptors, potentially increasing its biological activity.
– Position 15: Histidine is replaced with D-phenylalanine, another D-amino acid. This modification is intended to protect the peptide from further enzymatic breakdown.
– Position 27: Cysteine is substituted with N-methylglycine, also referred to as sarcosine. This alteration may extend the peptide’s half-life by mitigating enzymatic cleavage.
These modifications collectively aim to produce a peptide with increased stability, a longer half-life, and better-supported interaction with GHRH receptors compared to the original GRF (1-29). Modified GRF (1-29) is structurally identical to CJC-1295 without DAC. The DAC in CJC-1295 serves to modify its pharmacokinetic properties.
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