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. 2008 May;131(5):395–397. doi: 10.1085/jgp.200810012

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© 2008 Andersen

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jgp.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — Schematic representation of different, nonexclusive mechanisms by which one can drug an ion channel: (1) a drug may bind in the pore to block ion movement; (2) a drug may bind to a site wholly formed by the protein, to either inhibit or potentiate the channel function by altering the free energy difference between different channel states; (3) an amphiphilic drug may bind specifically to a defined site composed of both the protein and the bilayer lipids in which case its effects could also involve changes in the bilayer deformation energy associated with channel conformational changes; (4) an amphiphilic drug may accumulate nonspecifically at the protein/bilayer interface to alter local lipid packing, and thereby alter the bilayer deformation energy contribution to channel's conformational changes; and (5) an amphiphilic drug may adsorb at the lipid bilayer/solution interface to alter the bilayer deformation energy associated with the channel conformational changes.