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Three structural features are responsible for its selectivity profile: Aib at position 1 -aminoisobutyric acid introduces conformational rigidity at the N-terminus, restricting the peptides ability to engage receptors outside GHS-R1a D-2-naphthylalanine at position 3 the bulky aromatic sidechain optimizes fit within the GHS-R1a binding pocket while reducing cross-reactivity with receptors that mediate ACTH and prolactin release C-terminal amidation the amidated C-terminus improves metabolic stability and contributes to the selective receptor engagement profile Together, these modifications maximize GHS-R1a affinity while minimizing off-target interactions which is the structural explanation for why ipamorelin, at doses that robustly stimulate pituitary GH release, does not meaningfully activate the adrenocortical axis or prolactin-releasing pathways
The study did not distinguish between participants who regained lost weight and those who did not
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