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Two key structural features distinguish it from other GHRPs: (1) incorporation of an -aminoisobutyric residue (Aib) at position 1 replacing the histidine of classical GHRPs, stabilising the -turn conformation required for receptor activation, (2) presence of a D-2-naphthyl-alanine (D-2-Nal) at position 3 replacing the D-isomer tryptophan, increasing GHS-R1a selectivity over related receptors

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