Interaction of Primary Amphipathic Cell-Penetrating Peptides with Phospholipid-Supported Monolayers

• Published in: Langmuir 2004-10, Vol.20 (21), p.9255-9261
• Main Authors: Plénat, Thomas, Deshayes, Sébastien, Boichot, Sylvie, Milhiet, Pierre Emmanuel, Cole, Richard B, Heitz, Frédéric, Le Grimellec, Christian
• Format: Article
• Language: English
• Subjects: Membranes, Artificial; Particle Size; Peptides - chemical synthesis; Peptides - chemistry; Phospholipids - chemistry; Surface Properties
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la048622b

The mesoscopic organization adopted by two primary amphipathic peptides, P( β ) and P( α ), in Langmuir−Blodgett (LB) films made of either the pure peptide or peptide−phospholipid mixtures was examined by atomic force microscopy. P( β ), a potent cell-penetrating peptide (CPP), and P( α ) mainly differ by their conformational states, predominantly a β-sheet for P( β ) and an α-helix for P( α ), 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( β ) and filaments for P( α ), 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.