Matrix formalism for site-specific binding of unstructured proteins to multicomponent lipid membranes

Journal of Peptide Science : an Official Publication of the European Peptide Society
Vladimir B TeifAvinoam Ben-Shaul

Abstract

We describe a new approach to calculate the binding of flexible peptides and unfolded proteins to multicomponent lipid membranes. The method is based on the transfer matrix formalism of statistical mechanics recently described as a systematic tool to study DNA-protein-drug binding in gene regulation. Using the energies of interaction of the individual polymer segments with different membrane lipid species and the scaling corrections due to polymer looping, we calculate polymer adsorption characteristics and the degree of sequestration of specific membrane lipids. The method is applied to the effector domain of the MARCKS (myristoylated alanine rich C kinase substrate) protein known to be involved in signal transduction through membrane binding. The calculated binding constants of the MARCKS(151-175) peptide and a series of related peptides to mixed PC/PS/PIP2 membranes are in satisfactory agreement with in vitro experiments.

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Citations

Jul 20, 2010·Progress in Biophysics and Molecular Biology·Vladimir B Teif, Klemen Bohinc
May 27, 2008·Biophysical Journal·Shelly TzlilAvinoam Ben-Shaul
Oct 21, 2010·Biophysical Journal·Vladimir B TeifKarsten Rippe
Aug 8, 2018·Journal of Biomolecular Structure & Dynamics·Y V StirmanovY D Nechipurenko
Mar 20, 2008·Journal of Peptide Science : an Official Publication of the European Peptide Society·Miguel A R B Castanho, Margitta Dathe
Mar 10, 2011·Journal of Physics. Condensed Matter : an Institute of Physics Journal·Vladimir B Teif, Karsten Rippe
Jan 8, 2015·Journal of Physics. Condensed Matter : an Institute of Physics Journal·Vladimir B TeifKarsten Rippe

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