Lipid shape is a key factor for membrane interactions of amphipathic helical peptides-Reference-Cited by-同舟云学术

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Lipid shape is a key factor for membrane interactions of amphipathic helical peptides

Published:2012-07 Issue:7 Volume:1818 Page:1764-1776
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Strandberg Erik,Tiltak Deniz,Ehni Sebastian,Wadhwani Parvesh,Ulrich Anne S.

Funder

DFG-Center for Functional Nanostructures in Karlsruhe

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference91 articles.

1. Antimicrobial and cell penetrating peptides induce lipid vesicle fusion by folding and aggregation;Wadhwani;Eur. Biophys. J.,2012

2. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?;Brogden;Nat. Rev. Microbiol.,2005

3. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies;Hancock;Nat. Biotechnol.,2006

4. Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects;Wieprecht;Biochemistry,2000

5. NMR methods for studying membrane-active antimicrobial peptides;Strandberg;Concepts Magn. Reson. A,2004

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