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Titolo:
Solution structure of a novel ETB receptor selective agonist ET1-21[Cys(Acm)(1,15), Aib(3,11), Leu(7)] by nuclear magnetic resonance spectroscopy andmolecular 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:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 3, volume: 53, anno: 1999,
pagine: 223 - 233
SICI:
1397-002X(199903)53:3<223:SSOANE>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOTHELIN RECEPTOR; BINDING-SITES; VASOCONSTRICTOR PEPTIDE; PROTEIN CONFORMATIONS; PORCINE ENDOTHELIN; BIG ENDOTHELIN-1; CLONING; IDENTIFICATION; EXPRESSION; SUBTYPES;
Keywords:
endothelin-1; ETB agonist molecular modelling; NMR; solution structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
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., "Solution structure of a novel ETB receptor selective agonist ET1-21[Cys(Acm)(1,15), Aib(3,11), Leu(7)] by nuclear magnetic resonance spectroscopy andmolecular modelling", J PEPT RES, 53(3), 1999, pp. 223-233

Abstract

The solution structure of a biologically active modified linear endothelin-l analogue, ET1-21[Cys(Acm)(1,15), Aib(3,11), Leu(7)]. has been determinedfor the first time by two-dimensional nuclear magnetic resonance spectroscopy in a methanol-d(3)/water solvent mixture. Out of approximately one hundred linear peptide analogues tested by biological assay, this peptide, together with a dozen others, showed significant ETB selective agonist activity. Here we report the solution structure of an ETB selective agonist of a full-length, synthetic linear endothelin analogue. The calculated structures indicate that the peptide adopts an alpha-helical conformation between residues Ser(5)-His(16), whilst both N- and C-termini show no preferred conformation. These results suggest that the disulphide bridges normally associated with endothelin and sarafotoxin peptides may not necessarily be importantfor either ETB receptor binding activity or the formation of a helical conformation in solution.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/04/20 alle ore 23:09:28