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Titolo:
THREONINE(6)-BRADYKININ - MOLECULAR-DYNAMICS SIMULATIONS IN A BIPHASIC MEMBRANE MIMETIC
Autore:
PELLEGRINI M; MIERKE DF;
Indirizzi:
CLARK UNIV,GUSTAF H CARLSON SCH CHEM,950 MAIN ST WORCESTER MA 01610 CLARK UNIV,GUSTAF H CARLSON SCH CHEM WORCESTER MA 01610 UNIV PADUA,BIOPOLYMER RES CTR,DEPT ORGAN CHEM I-35131 PADUA ITALY UNIV MASSACHUSETTS,MED CTR,DEPT PHARMCOL & MOL TOXICOL WORCESTER MA 01655
Titolo Testata:
Journal of medicinal chemistry
fascicolo: 1, volume: 40, anno: 1997,
pagine: 99 - 104
SICI:
0022-2623(1997)40:1<99:T-MSIA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
BIOLOGICAL-ACTIVITY; LIPID-MEMBRANES; PEPTIDES; MICELLES; CONFORMATION; NMR; ORIENTATION; RECEPTOR; DODECYLPHOSPHOCHOLINE; LOCATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
M. Pellegrini e D.F. Mierke, "THREONINE(6)-BRADYKININ - MOLECULAR-DYNAMICS SIMULATIONS IN A BIPHASIC MEMBRANE MIMETIC", Journal of medicinal chemistry, 40(1), 1997, pp. 99-104

Abstract

The natural peptide [Thr(6)]-bradykinin, (2)-Pro(3)-Gly(4)-Phe(5)Thr(6)-PrO7-Phe(8)-Arg(9), has been conformationally examined by moleculardynamics simulations using a two-phase box consisting of H2O and CCl4to mimic the micellar environment utilized in the H-1-NMR studies. The different conformations generated from distance geometry calculations were refined with extensive molecular dynamics simulations. The resulting conformations provide additional structural insight into the differing biological activities of native bradykinin and [Thr(6)]-bradykinin, produced by the one conservative substitution Thr(6) for Ser(6). In addition, the simulations give some indication of the interaction of the peptide with the biphasic, hydrophilic/hydrophobic environment of the micelle. Such information is vital given the accumulating data indicating that the peptide first interacts with the membrane before the membrane-bound receptor. The structures of membrane-bound [Thr(6)]-bradykinin developed here provide experimental support for the interaction of residues 7 and 8 with the core of the membrane-bound receptor and the N-terminus and C-terminal arginine interacting with the extracellular portion of the receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 20:10:18