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Biophys J, August 1999, p. 739-746, Vol. 77, No. 2

Distinctly Different Interactions of Anesthetic and Nonimmobilizer with Transmembrane Channel Peptides

Pei Tang, Jian Hu, Serguei Liachenko, and Yan Xu

Department of Anesthesiology and Critical Care Medicine, Department of Pharmacology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261 USA

Although it plays no clinical role in general anesthesia, gramicidin A, a transmembrane channel peptide, provides an excellent model for studying the specific interaction between volatile anesthetics and membrane proteins at the 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 µM gramicidin A in a vesicle suspension of 60 mM phosphatidylcholine-phosphatidylglycerol (PC/PG), the intermolecular cross-relaxation rate constants between 19F of F3 and 1H in the chemical shift regions for the indole and backbone amide 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 F6 and protons in these regions. Sodium transport study showed that with 75 µM gramicidin A in a vesicle suspension of 66 mM PC/PG, F3 increased the 23Na apparent efflux rate constant from 149.7 ± 7.2 of control (n = 3) to 191.7 ± 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 of importance to general anesthesia.

Biophys J, August 1999, p. 739-746, Vol. 77, No. 2
© 1999 by the Biophysical Society   0006-3495/99/08/739/08  $2.00


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