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Structure‐activity relationship for peptídic growth hormone secretagogues
Author(s) -
Ferro P.,
Krotov G.,
Zvereva I.,
Rodchenkov G.,
Segura J.
Publication year - 2017
Publication title -
drug testing and analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.065
H-Index - 54
eISSN - 1942-7611
pISSN - 1942-7603
DOI - 10.1002/dta.1947
Subject(s) - chemistry , receptor , ghrelin , medicine , endocrinology , in vivo , growth hormone , hormone , biological activity , in vitro , biochemistry , biology , microbiology and biotechnology
Growth hormone releasing peptides (GHRPs) could be widely used by cheating athletes because they produce growth hormone (GH) secretion, so may generate an ergogenic effect in the body. Knowledge of the essential amino acids needed in GHRP structure for interaction with the target biological receptor GHSR1a, the absorption through different administration routes, and the maintenance of pharmacological activity of potential biotransformation products may help in the fight against their abuse in sport. Several GHRPs and truncated analogues with the common core Ala‐Trp‐(D‐Phe)‐Lys have been studied with a radio‐competitive assay for the GHSR1a receptor against the radioactive natural ligand ghrelin. Relevant chemical modifications influencing the activity for positions 1, 2, 3, and 7 based on the structure aa‐aa‐aa‐Ala‐Trp‐(D‐Phe)‐Lys have been obtained. To test in vivo the applicability of the activities observed, the receptor assay activity in samples from excretion studies performed after nasal administration of GHRP‐1, GHRP‐2, GHRP‐6, Hexarelin, and Ipamorelin was confirmed. Overall results obtained allow to infer structure‐activity information for those GHRPs and to detect GHSR1a binding (intact GHRPs plus active metabolites) in excreted urines. Copyright © 2016 John Wiley & Sons, Ltd.