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Charge-Dependent Translocation of the Trojan Peptide Penetratin across Lipid Membranes

Department of Biophysical Chemistry, Umeå University, SE-90187 Umeå, Sweden

Correspondence: Address reprint requests to Hans Binder, Interdisciplinary Centre for Bioinformatics of Leipzig University, D-4103 Leipzig, Kreuzstr. 7b. Fax: +49-341-1495-119; E-mail: binder{at}rz.uni-leipzig.de.

We studied the interaction of the cell-penetrating peptide penetratin with mixed dioleoylphosphatidylcholine/dioleoylphoshatidylglycerol (DOPC/DOPG) unilamellar vesicles as a function of the molar fraction of anionic lipid, X_PG, by means of isothermal titration calorimetry. The work was aimed at getting a better understanding of factors that affect the peptide binding to lipid membranes and its permeation through the bilayer. The binding was well described by a surface partitioning equilibrium using an effective charge of the peptide of z_P 5.1 ± 0.5. The peptide first binds to the outer surface of the vesicles, the effective binding capacity of which increases with X_PG. At X_PG 0.5 and a molar ratio of bound peptide-to-lipid of 1/20 the membranes become permeable and penetratin binds also to the inner monolayer after internalization. The results were rationalized in terms of an "electroporation-like" mechanism, according to which the asymmetrical distribution of the peptide between the outer and inner surfaces of the charged bilayer causes a transmembrane electrical field, which alters the lateral and the curvature stress acting within the membrane. At a threshold value these effects induce internalization of penetratin presumably via inversely curved transient structures.

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