Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations

Authors

  • Burkhard Bechinger

    Corresponding author
    1. Institut de Chimie, Université de Strasbourg/CNRS, UMR7177, 4, rue Blaise Pascal, 67070 Strasbourg, France
    • Faculté de chimie, Institut le Bel, 4, rue Blaise Pascal, 67070 Strasbourg, France.
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Errata

This article is corrected by:

  1. Errata: Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations Volume 21, Issue 8, 689, Article first published online: 22 July 2015

  • Special issue devoted to contributions presented at the 12th Naples Worshop on Bioactive Peptides and 2nd Italy-Korea Symposium on Antimicrobial Peptides, 4-7 June 2010, Naples, Italy.

Abstract

In order to better understand the mechanisms of action of linear cationic host defense peptides, biophysical and structural investigations of their interactions with membranes and with other biomacromolecules are reviewed. In particular, an extensive overview will be given of the topological studies of magainins in a number of different lipid environments. Furthermore, amphipathic helices have been designed in such a manner to allow the easy control of their membrane alignment. These peptides not only exhibit potent antimicrobial and transfection activities, but their investigation has also provided important insights into mechanistic aspects of their biological functions. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.

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