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Titolo:
Distinctly different interactions of anesthetic and nonimmobilizer with transmembrane channel peptides
Autore:
Tang, P; Hu, J; Liachenko, S; Xu, Y;
Indirizzi:
Univ Pittsburgh, Dept Anesthesiol & Crit Care Med, Pittsburgh, PA 15261 USA Univ Pittsburgh Pittsburgh PA USA 15261 are Med, Pittsburgh, PA 15261 USA Univ Pittsburgh, Dept Pharmacol, Pittsburgh, PA 15261 USA Univ PittsburghPittsburgh PA USA 15261 armacol, Pittsburgh, PA 15261 USA
Titolo Testata:
BIOPHYSICAL JOURNAL
fascicolo: 2, volume: 77, anno: 1999,
pagine: 739 - 746
SICI:
0006-3495(199908)77:2<739:DDIOAA>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; NICOTINIC ACETYLCHOLINE-RECEPTOR; MEYER-OVERTON HYPOTHESIS; GRAMICIDIN-A CHANNEL; PHOSPHOLIPID-VESICLES; MEMBRANE-PROTEINS; LIPID-MEMBRANES; ION-TRANSPORT; NMR; SITES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Tang, P Univ Pittsburgh, Dept Anesthesiol & Crit Care Med, W-1357 Biomed Sci Tower, Pittsburgh, PA 15261 USA Univ Pittsburgh W-1357 Biomed Sci Tower Pittsburgh PA USA 15261 SA
Citazione:
P. Tang et al., "Distinctly different interactions of anesthetic and nonimmobilizer with transmembrane channel peptides", BIOPHYS J, 77(2), 1999, pp. 739-746

Abstract

Although it plays no clinical role in general anesthesia, gramicidin A, a transmembrane channel peptide, provides an excellent model for studying thespecific interaction between volatile anesthetics and membrane proteins atthe molecular level. We show here that a pair of structurally similar volatile anesthetic and nonimmobilizer (nonanesthetic), 1-chloro-1,2,2-trifluorocyclobutane (F3) and 1,2-dichlorohexafluorocyclobutane (F6), respectively,interacts differently with the transmembrane peptide. With 400 mu M gramicidin A in a vesicle suspension of 60 mM phosphatidylcholine-phosphatidylglycerol (PC/PG), the intermolecular cross-relaxation rate constants between F-19 of F3 and H-1 in the chemical shift regions for the indole and backboneamide protons were 0.0106 +/- 0.0007 (n = 12) and 0.0105 +/- 0.0014 (n = 8) s(-1), respectively. No cross-relaxation was measurable between 19F of F6and protons in these regions. Sodium transport study showed that with 75 mu M gramicidin A in a vesicle suspension of 66 mM PC/PG, F3 increased the Na-23 apparent efflux rate constant from 149.7 +/- 7.2 of control (n = 3) to191.7 +/- 12.2 s(-1) (n = 3), and the apparent influx rate constant from 182.1 +/- 15.4 to 222.8 +/- 21.7 s(-1) (n = 3). In contrast, F6 had no effects on either influx or efflux rate. It is concluded that the ability of general anesthetics to interact with amphipathic residues near the peptide-lipid-water interface and the inability of nonimmobilizer to do the same may represent some characteristics of anesthetic-protein interaction that are ofimportance to general anesthesia.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:07:30