Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Langmuir. 2004 Oct 12;20(21):9255-61.

Interaction of primary amphipathic cell-penetrating peptides with phospholipid-supported monolayers.

Author information

  • 1Nanostructures et Complexes Membranaires, CBS, CNRS UMR5048-INSERM U554, 29 rue de Navacelles, 34090 Montpellier Cedex, France.

Abstract

The mesoscopic organization adopted by two primary amphipathic peptides, P(beta) and P(alpha), in Langmuir-Blodgett (LB) films made of either the pure peptide or peptide-phospholipid mixtures was examined by atomic force microscopy. P(beta), a potent cell-penetrating peptide (CPP), and P(alpha) mainly differ by their conformational states, predominantly a beta-sheet for P(beta) and an alpha-helix for P(alpha), as determined by Fourier transform infrared spectroscopy. LB films of pure peptide, transferred significantly below their collapse pressure, were characterized by the presence of supramolecular structures, globular aggregates for P(beta) and filaments for P(alpha), inserted into the monomolecular film. In mixed peptide-phospholipid films, similar structures could be observed, as a function of the phospholipid headgroup and acyl chain saturation. They often coexisted with a liquid-expanded phase composed of miscible peptide-lipid. These data strongly suggest that primary amphipathic CPP and antimicrobial peptides may share, to some extent, common mechanisms of interaction with membranes.

Copyright 2004 American Chemical Society

PMID:
15461515
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for American Chemical Society
    Loading ...
    Write to the Help Desk