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. 1995 Nov 21;92(24):11165–11169. doi: 10.1073/pnas.92.24.11165

Growth hormone secretagogues: characterization, efficacy, and minimal bioactive conformation.

R S McDowell 1, K A Elias 1, M S Stanley 1, D J Burdick 1, J P Burnier 1, K S Chan 1, W J Fairbrother 1, R G Hammonds 1, G S Ingle 1, N E Jacobsen 1, et al.
PMCID: PMC40592  PMID: 7479958

Abstract

Another class of growth hormone (GH) secretagogues has been discovered by altering the backbone structure of a flexible linear GH-releasing peptide (GHRP). In vitro and in vivo characterization confirms these GH secretagogues as the most potent and smallest (M(r) < 500) reported. Anabolic efficacy is demonstrated in rodents with intermittent delivery. A convergent model of the bioactive conformation of GHRPs is developed and is supported by the NMR structure of a highly potent cyclic analog of GHRP-2. The model and functional data provide a logical framework for the further design of low-molecular weight secretagogues and illustrate the utility of an interdisciplinary approach to elucidating potential bound-state conformations of flexible peptide ligands.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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