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Probing the interaction forces between hydrophobic peptides and supported lipid bilayers using AFM
Author(s) -
Andre Guillaume,
Brasseur Robert,
Dufrêne Yves F.
Publication year - 2007
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.837
Subject(s) - atomic force microscopy , lipid bilayer , nanotechnology , chemistry , materials science , biophysics , membrane , biochemistry , biology
Despite the vast body of literature that has accumulated on tilted peptides in the past decade, direct information on the forces that drive their interaction with lipid membranes is lacking. Here, we attempted to use atomic force microscopy (AFM) to explore the interaction forces between the Simian immunodeficiency virus peptide and phase‐separated supported bilayers composed of various lipids, i.e. dipalmitoylphosphatidylcholine, dioleoylphosphatidylcholine, dioleoylphosphatidic acid and dipalmitoylphosphatidylethanolamine. Histidine‐tagged peptides were attached onto AFM tips terminated with nitrilotriacetate and tri(ethylene glycol) groups, an approach expected to ensure optimal exposure of the C‐terminal hydrophobic domain. Force–distance curves recorded between peptide‐tips and the different bilayer domains always showed a long‐range repulsion upon approach and a lack of adhesion upon retraction, in marked contrast with the hydrophobic nature of the peptide. To explain this unexpected behaviour, we suggest a mechanism in which lipids are pulled out from the bilayer due to strong interactions with the peptide‐tip, in agreement with the very low force needed to extract lipids from supported bilayers. Copyright © 2007 John Wiley & Sons, Ltd.