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* Department of Physics, National Central University, Chung-Li, Taiwan 32054 ROC; and Department of Physics & Astronomy, Rice University, Houston, Texas 77251 USA
Correspondence: Address reprint requests to Dr. Huey W. Huang, Department of Physics & Astronomy, Rice University, Houston, Texas 77251-1892. Tel.: 713-348-4899; Fax: 713-348-4150; E-mail: hwhuang{at}rice.edu; or Dr. Fang-Yu Chen, Department of Physics, National Central University, Chung-Li, Taiwan 32054. Tel.: 886-3-4227151 x5331; Fax: 886-3-4251175; E-mail: fychen{at}joule.phy.ncu.edu.tw.
Antimicrobial peptides have two binding states in a lipid bilayer, a surface state S and a pore-forming state I. The transition from the S state to the I state has a sigmoidal peptide-concentration dependence indicating cooperativity in the peptide-membrane interactions. In a previous paper, we reported the transition of alamethicin measured in three bilayer conditions. The data were explained by a free energy that took into account the membrane thinning effect induced by the peptides. In this paper, the full implications of the free energy were tested by including another type of peptide, melittin, that forms toroidal pores, instead of barrel-stave pores as in the case of alamethicin. The S-to-I transitions were measured by oriented circular dichroism. The membrane thinning effect was measured by x-ray diffraction. All data were in good agreement with the theory, indicating that the membrane thinning effect is a plausible mechanism for the peptide-induced pore formations.
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