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Biophys. J. BioFAST: First Published March 11, 2005. doi:10.1529/biophysj.104.055566
© 2005 by the Biophysical Society.

A more recent version of this article appeared on June 1, 2005.
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BIOPHYSICAL THEORY AND MODELING

MD simulations of C2F6 effects on gramicidin A: Implication of mechanisms of general anesthesia

Zhanwu Liu 1, Yan Xu 1 and Pei Tang 1*

1 University of Pittsburgh

* To whom correspondence should be addressed. E-mail: tangp{at}anes.upmc.edu.

Submitted on November 1, 2004
Revised on December 22, 2004
Accepted on 8 March 2005


  Abstract
It was recently postulated that the effects of general anesthetics on protein global dynamics might underlie a unitary molecular mechanism of general anesthesia (Tang & Xu, Proc Natl Acad Sci USA, 99:16035-40, 2002). To verify that the specific dynamics effects caused by general anesthetics were not shared by non-anesthetic molecules, two parallel 8-ns all-atom molecular dynamics simulations were performed on a gramicidin (gA) channel in a fully hydrated dimyristoylphosphatidylcholine (DMPC) membrane in the presence and absence of hexafluoroethane (HFE), which structurally resembles the potent anesthetic molecule halothane but produces no anesthesia. Similar to halothane, HFE had no measurable effects on the gA channel structure. In contrast to halothane, HFE produced no significant changes in the gA channel dynamics. The difference between halothane and HFE on channel dynamics can be attributed to their distinctly different distributions within the lipid bilayer and consequently to the different interactions of the anesthetic and the non-anesthetic molecules with the channel-anchoring tryptophan residues. The study further supports the notion that anesthetic-induced changes in protein global dynamics may play an important role in mediating anesthetic actions on proteins.

Key Words: Mechanisms of general anesthesia, anesthetic effects, gramicidin A, hexafluoroethane, ion channels, molecular dynamics simulations




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Copyright © 2005 by the Biophysical Society.