The GHRH biology that ties all three together
Native human growth-hormone-releasing hormone (GHRH) is a 44-amino-acid peptide secreted by the hypothalamus. It travels through the hypothalamic-pituitary portal circulation, binds the GHRH receptor on somatotrophs in the anterior pituitary, and triggers the release of growth hormone (GH) into systemic circulation. That receptor — a G-protein-coupled receptor with a specific affinity profile for the N-terminal region of GHRH — is the shared target of every molecule in this comparison.[1][10]
Biochemistry shows that the first 29 amino acids of GHRH (the 'GHRH 1-29' fragment) carry the full biological activity of the parent peptide on the GHRH receptor. That observation is the historical reason this whole class of analogues exists: if you can keep the first 29 residues and stabilise them against proteolytic degradation, you have a GHRH-like molecule that is easier to make, easier to characterise, and longer-lasting than the native 44-mer.[1][2]
Three different design philosophies sit on top of that biology. Sermorelin keeps the bare GHRH 1-29 sequence. CJC-1295 takes GHRH 1-29 and modifies it for protease resistance and (in the DAC variant) plasma persistence. Tesamorelin keeps the full 1-44 length of native GHRH and adds a lipophilic N-terminal modification to slow degradation. Same receptor, three different engineering answers.[1][2][4][5]
