Background reading on the GHRH-analogue family (sermorelin, tesamorelin, CJC-1295 with and without DAC) and the small-peptide ghrelin mimetics (Ipamorelin, hexarelin, GHRP-2/6). Sequences, half-life modifications, receptor selectivity, and the literature on their use as research probes.
GHRH analogues are synthetic peptides modelled on the 44-residue native growth-hormone-releasing hormone, typically truncated to the bioactive 1–29 fragment (sermorelin) and modified for stability. CJC-1295 introduces four amino-acid substitutions to resist proteolytic degradation; the DAC variant adds a maleimidopropionyl group that binds covalently to serum albumin in vivo, extending half-life from minutes to days. Tesamorelin is a related GRF(1–44) analogue with N-terminal hexenoyl modification.
Ghrelin-mimetic secretagogues are unrelated to GHRH structurally — they bind GHS-R1a (the ghrelin receptor) instead of the GHRH receptor. Ipamorelin (a five-residue Aib-His-D-2-Nal-D-Phe-Lys-NH2 sequence) was characterized as the first selective GH secretagogue, with minimal effect on ACTH, cortisol, FSH, LH, or TSH. Co-administered GHRH analogues plus ghrelin mimetics produce additive effects in vitro because they act via two distinct receptor systems.
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