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Titolo:
A linear endothelin-1 analogue: solution structure of ET-1[Aib(1,3,11,15),Nle(7)] by nuclear magnetic resonance spectroscopy and molecular modelling
Autore:
Hewage, CM; Jiang, L; Parkinson, JA; Ramage, R; Sadler, IH;
Indirizzi:
Univ Edinburgh, Dept Chem, Edinburgh EH9 3JJ, Midlothian, Scotland Univ Edinburgh Edinburgh Midlothian Scotland EH9 3JJ Midlothian, Scotland
Titolo Testata:
NEUROCHEMISTRY INTERNATIONAL
fascicolo: 1, volume: 35, anno: 1999,
pagine: 35 - 45
SICI:
0197-0186(199907)35:1<35:ALEASS>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
SOLUTION CONFORMATION; PROTEIN CONFORMATIONS; BIOLOGICAL-ACTIVITY; DISTANCE GEOMETRY; PEPTIDE FAMILY; RECEPTOR; CLONING; H-1-NMR; CDNA; RAT;
Keywords:
endothelin-1; ET-1; molecular modelling; NMR; solution structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Sadler, IH Univandinburgh, Dept Chem, W Mains Rd, Edinburgh EH9 3JJ, Midlothian, Scotl Univ Edinburgh W Mains Rd Edinburgh Midlothian Scotland EH9 3JJ
Citazione:
C.M. Hewage et al., "A linear endothelin-1 analogue: solution structure of ET-1[Aib(1,3,11,15),Nle(7)] by nuclear magnetic resonance spectroscopy and molecular modelling", NEUROCHEM I, 35(1), 1999, pp. 35-45

Abstract

Two-dimensional nuclear magnetic resonance techniques and a combination ofdistance geometry and molecular dynamics calculations were utilised to determine the three dimensional solution structure of an ET-1 analogue, ET-1[Aib(1,3,11,5), Nle(7)], in a methanol-d(3)/water co-solvent. The modelled structure shows that the peptide folds into a consistent alpha-helical conformation between residues Ser(4)-His(16) while the C-terminus prefers no fixed conformation. Our studies cofirm that the disulphide links which are normally associated with the endothelin family of neuropeptides are not important for the formation of a helical conformation in solution. This full length, modified, synthetic linear ET-1 analogue plays a vital role towards designing endothelin receptor agonists. Structure activity relationships are discussed in terms of the conformational features of the calculated structure. (C) 1999 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 15:31:46