Interaction of amphipathic alpha-helical peptides with a lipid membrane: Adsorption and pore formation
Artikel i vetenskaplig tidskrift, 2014

Amphipathic alpha-helical peptides often exhibit antimicrobial or antiviral properties. Adsorption of such peptides at a lipid membrane may result in pore formation. Current phenomenological models of the latter process imply that the peptide-peptide lateral interaction is repulsive and that the conditions for pore formation depend on the difference of the peptide energies at the membrane surface and in a pore. There is, however, experimental evidence that the kinetics of peptide adsorption at small vesicles (about 100 nm diameter) may be cooperative and accordingly the peptide-peptide lateral interaction may be attractive. In addition, the experiments indicate that the peptide-induced pore formation is often observed at the conditions close to those corresponding to pore formation under externally induced tensile stress where the difference of the peptide energies at the membrane surface and in a pore is irrelevant. Here, a model describing both types of peptide-peptide lateral interactions at a membrane is proposed. In addition, a new scenario of peptide-induced pore formation naturally explaining the similarity of this process under different conditions is suggested. (c) 2014 Elsevier B.V. All rights reserved.

KINETICS

MODEL

BILAYERS

Antimicrobial and antiviral peptides

Pore formation

ANTIMICROBIAL PEPTIDES

VESICLES

Membrane strain

Lateral interactions

Lipid bilayers

MECHANISM

Författare

Vladimir Zhdanov

Chalmers, Teknisk fysik, Biologisk fysik

Physica A: Statistical Mechanics and its Applications

0378-4371 (ISSN)

Vol. 401 45-51

Ämneskategorier

Fysik

Biofysik

DOI

10.1016/j.physa.2014.01.028