| Literature DB >> 7479958 |
R S McDowell1, K A Elias, M S Stanley, D J Burdick, J P Burnier, K S Chan, W J Fairbrother, R G Hammonds, G S Ingle, N E Jacobsen, D L Mortensen, T E Rawson, W B Won, R G Clark, T C Somers.
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.Entities:
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Year: 1995 PMID： 7479958 PMCID： PMC40592 DOI： 10.1073/pnas.92.24.11165
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205