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Implicit Solvent Simulations of Peptide Interactions with Anionic Lipid Membranes by Themis Lazaridis is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract A recently developed implicit membrane model (IMM1) is supplemented with a Gouy–Chapman term describing counterion‐screened electrostatic interactions of a solute with negatively charged membrane lipids. The new model is tested on peptides that bind to anionic membranes. Pentalysine binds just outside the plane of negative charge, whereas Lys‐Phe peptides insert their aromatic rings into the hydrophobic core. Melittin and magainin 2 bind more strongly to anionic than to neutral membranes and in both cases insert their hydrophobic residues into the hydrocarbon core. The third domain of __Antennapedia__ homeodomain (penetratin) binds as an α‐helix in the headgroup region. Cardiotoxin II binds strongly to anionic membranes but marginally to neutral ones. In all cases, the location and configuration of the peptides are consistent with experimental data, and the effective energy changes upon binding compare favorably with experimental binding free energies. The model opens the way to exploring the effect of membrane charge on the location, conformation, and dynamics of a large variety of biologically active peptides on membranes. Proteins 2005. © 2004 Wiley‐Liss, Inc.

Who reads Implicit Solvent Simulations of Peptide Interactions with Anionic Lipid Membranes?

Author

Themis Lazaridis

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)