Peptide-induced domain formation in supported lipid bilayers: direct evidence by combined atomic force and polarized total internal reflection fluorescence microscopy.
Direct visualization of the mechanism(s) by which peptides induce localized changes to the structure of membranes has high potential for enabling understanding of the structure-function relationship in antimicrobial and cell-penetrating peptides. We have applied a combined imaging strategy to track the interaction of a model antimicrobial peptide, PFWRIRIRR-amide, with bacterial membrane-mimetic supported phospholipid bilayers comprised of POPE/TOCL. Our in situ studies revealed rapid reorganization of the POPE/TOCL membrane into localized TOCL-rich domains with a concomitant change in the organization of the membranes themselves, as reflected by changes in fluorescent-membrane-probe order parameter, upon introduction of the peptide.
Oreopoulos
John
J
Institute of Biomaterials and Biomedical Engineering, Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Ontario, Canada.
Epand
Raquel F
RF
Epand
Richard M
RM
Yip
Christopher M
CM
D000042:Absorption; D000818:Animals; D002417:Cattle; D005456:Fluorescent Dyes / Q000737:chemistry; D008051:Lipid Bilayers / Q000378:metabolism*; D008055:Lipids / Q000737:chemistry; D021962:Membrane Microdomains / Q000187:drug effects*; D018625:Microscopy, Atomic Force / Q000379:methods*; D008856:Microscopy, Fluorescence / Q000379:methods*; D010455:Peptides / Q000494:pharmacology*; D013997:Time Factors
D005456:Fluorescent Dyes; D008051:Lipid Bilayers; D008055:Lipids; D010455:Peptides