Growth hormone secretagogues: characterization, efficacy, and minimal bioactive conformation
| Autor: | R S, McDowell, 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 |
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| Rok vydání: | 1995 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Molecular Sequence Data Peptide Biology Peptides Cyclic Protein Structure Secondary Rats Sprague-Dawley Structure-Activity Relationship In vivo Pituitary Gland Anterior Consensus Sequence Structure–activity relationship Animals Amino Acid Sequence Peptide sequence chemistry.chemical_classification Oligopeptide Multidisciplinary Nuclear magnetic resonance spectroscopy In vitro Hormones Rats Biochemistry chemistry Growth Hormone Female Secretory Rate Oligopeptides Hormone Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 92(24) |
| ISSN: | 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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