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Titolo:
H-1 NMR structural analysis of human ghrelin and its six truncated analogs
Autore:
Elipe, MVS; Bednarek, MA; Gao, YD;
Indirizzi:
Merck Res Labs, Dept Drug Metab, Rahway, NJ USA Merck Res Labs Rahway NJ USA k Res Labs, Dept Drug Metab, Rahway, NJ USA Merck Res Labs, Dept Med Chem, Rahway, NJ USA Merck Res Labs Rahway NJ USA rck Res Labs, Dept Med Chem, Rahway, NJ USA
Titolo Testata:
BIOPOLYMERS
fascicolo: 7, volume: 59, anno: 2001,
pagine: 489 - 501
SICI:
0006-3525(200112)59:7<489:HNSAOH>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-HORMONE SECRETAGOGUE; ACYLATED PEPTIDE; RECEPTOR; RATS; PITUITARY; RELEASE; STOMACH; HEXAPEPTIDE; SECRETION; SEQUENCE;
Keywords:
H-1 NMR; CD; human ghrelin; ghrelin analogs; growth hormone-releasing peptide-6; molecular modeling;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Elipe, MVS Merck Res Labs, Dept Drug Metab, Rahway, NJ USA Merck Res LabsRahway NJ USA Dept Drug Metab, Rahway, NJ USA
Citazione:
M.V.S. Elipe et al., "H-1 NMR structural analysis of human ghrelin and its six truncated analogs", BIOPOLYMERS, 59(7), 2001, pp. 489-501

Abstract

Human ghrelin, the first recognized natural ligand (if growth hormone secretagogue growth hormone secretagogue receptors (GHS-Rs) (M. Kojima, H. Hosada, Y. Date, M. Nakazato, H. Matsuo, and K. Kangawa, Nature, 1999, Vol. 402, pp. 656-660), consists of 28 amino acids of which Ser3 is modified by n-octanoylation. This new peptide hormone has been implicated not only in regulation of the GH secretion but also in regulation of food intake, The discovery of ghrelin opens up more opportunities to study the relationship of ghrelin with metabolic diseases. Until now, only mass spectometry, analysis has been reported on the structure of ghrelin. NMR analysis is a suitable way to study if any tertiary structure of unbound ghrelin is present in solution. NMR studies were carried out on human ghrelin and its five truncated analogs. The full-length ghrelin and its fragments exhibited random coil behavior in aqueous solution. Additional studies were carried out on the shortest active segment of human ghrelin, which consists of the first five aminoacids of the ghrelin sequence (M. A. Bednarek. S. D. Feighner, S.-S. Pong,K. K. McKee, D. L. Hreniuk, M. V. Silva, V A. Warrem, A. D. Howard, L. H. Y. Van der Ploeg, and J. V Heck, Journal of Medical Chemistry, 2000, Vol. 43, pp. 4370-4376). to compare the spectral features with their counterpartsit? the full-length ghrelin. The NMR data showed behavior similar to ghrelin except for two additional nuclear Overhauser effects (NOEs) between the Phe4 NH and the protons of the beta -methylene of Ser3. CD on human ghrelinand its short active analog in water were indicative of random coil peptides. Molecular modeling based on NMR data was carried out to probe which structural features were similar to growth hormone-releasing peptide-6 (GHRP-6), a hexapeptide that binds to GHS-R releasing GH and stimulating food intake. Modeling suggested some similarities, but they were not of a nature to account for binding properties of these compounds. (C) 2001 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 05:58:23