Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The role of backbone conformation in deltorphin II binding: A QSAR study of new analogues modified in the 5-, 6-positions of the address domain
Autore:
Schullery, SE; Rodgers, DW; Tripathy, S; Jayamaha, DE; Sanvordekar, MD; Renganathan, K; Mousigian, C; Heyl, DL;
Indirizzi:
Eastern Michigan Univ, Dept Chem, Ypsilanti, MI 48197 USA Eastern MichiganUniv Ypsilanti MI USA 48197 hem, Ypsilanti, MI 48197 USA Univ Michigan, Coll Pharm, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 Coll Pharm, Ann Arbor, MI 48109 USA
Titolo Testata:
BIOORGANIC & MEDICINAL CHEMISTRY
fascicolo: 10, volume: 9, anno: 2001,
pagine: 2633 - 2642
SICI:
0968-0896(200110)9:10<2633:TROBCI>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
DELTA-OPIOID RECEPTOR; MORPHINE-TOLERANCE; PHYSICAL-DEPENDENCE; AMPHIBIAN SKIN; LIGAND-BINDING; HIGH-AFFINITY; SIDE-CHAINS; PEPTIDES; DERMENKEPHALIN; MU;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Heyl, DL Eastern Michigan Univ, Dept Chem, Ypsilanti, MI 48197 USA EasternMichigan Univ Ypsilanti MI USA 48197 lanti, MI 48197 USA
Citazione:
S.E. Schullery et al., "The role of backbone conformation in deltorphin II binding: A QSAR study of new analogues modified in the 5-, 6-positions of the address domain", BIO MED CH, 9(10), 2001, pp. 2633-2642

Abstract

The delta selectivity of the opioid heptapeptides deltorphin I and II has been attributed to the C-terminal 'address' domain, the hydrophobic Val(5)-Val(6) residues apparently playing a topographical role. We now report the synthesis, opioid binding affinities, and a QSAR study of a series of peptides in which one of the valine side chains was altered. QSAR analyses included previously published models for a binding pocket interaction and an optimum size (Schullery, S.; Mohammedshah, T.; Makhlouf, R.; Marks, E.; Wilenkin, B.; Escobar, S., Mousigian, C.; Heyl, D. Bioorg. Med. Chem. 1997, 5, 2221), and a new approach for backbone conformational effects using Langevin dynamics simulation (PM3 semi-empirical force field) of an isolated peptidefragment containing the side chain and flanking peptide bonds. No evidenceis found of binding pocket interactions or optimum size for either the position-5 or -6 side chain. Rather, 5 binding is generally disfavored while lt binding is either unaffected (position-5) or favored (position-6) by larger side chains, The dynamics results provide evidence of similar 'local' conformation roles for the positions 5 and 6 side chains. Specifically, deltabinding is favored by side chains that maximize the extension of the backbone, measured as the through-space distance between peptide fragment ends, the angle between lines connecting the a-carbon with fragment ends, or the difference between the psi and phi peptide angles. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 04:17:52