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Biophys. J. BioFAST: First Published October 27, 2006. doi:10.1529/biophysj.106.098681
© 2006 by the Biophysical Society.

A more recent version of this article appeared on January 1, 2007.
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BIOPHYSICAL LETTERS

SGTx1, a Kv Channel Gating-Modifier Toxin, Binds to the Interfacial Region of Lipid Bilayers

Chze Ling Wee 1, Daniele Bemporad 2, Zara Sands 1, David Gavaghan 1 and Mark S.P. Sansom 3*

1 Univ Oxford
2 Johnson and Johnson Pharmaceutical Research and Developmen
3 University of Oxford

* To whom correspondence should be addressed. E-mail: mark.sansom{at}bioch.ox.ac.uk.

Submitted on October 2, 2006
Revised on October 11, 2006
Accepted on 18 October 2006


  Abstract
SGTx1 is a gating-modifier toxin that has been shown to inhibit the potassium voltage-gated (Kv) channel Kv2.1. SGTx1 is thought to bind to the S3b-S4a region of the voltage-sensor (VS), and is believed to alter the energetics of gating. Gating-modifier toxins such as SGTx1 are of interest as they can be used to probe the structure and dynamics of their target channels. Although there are experimental data for SGTx1, its interaction with lipid bilayer membranes remains to be characterized. We performed atomistic and coarse-grained (CG) molecular dynamics (MD) simulations to study the interaction of SGTx1 with a POPC and a 3:1 POPE/POPG lipid bilayer membrane. We reveal the preferential partitioning of SGTx1 into the water/membrane interface of the bilayer. We also show that electrostatic interactions between the charged residues of SGTx1 and the lipid headgroups play an important role in stabilizing SGTx1 in a bilayer environment.

Key Words: coarse grained, molecular dynamics, potassium channel, simulations, toxin, voltage sensor




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Copyright © 2006 by the Biophysical Society.