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PubMed · 15454442

Using the atomic force microscope to study the interaction between two solid supported lipid bilayers and the influence of synapsin I.

Ioana Pera·Rüdiger Stark·Michael Kappl·Hans-Jürgen Butt·Fabio Benfenati
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Abstract

To measure the interaction between two lipid bilayers with an atomic force microscope one solid supported bilayer was formed on a planar surface by spontaneous vesicle fusion. To spontaneously adsorb lipid bilayers also on the atomic force microscope tip, the tips were first coated with gold and a monolayer of mercapto undecanol. Calculations indicate that long-chain hydroxyl terminated alkyl thiols tend to enhance spontaneous vesicle fusion because of an increased van der Waals attraction as compared to short-chain thiols. Interactions measured between dioleoylphosphatidylcholine, dioleoylphosphatidylserine, and dioleoyloxypropyl trimethylammonium chloride showed the electrostatic double-layer force plus a shorter-range repulsion which decayed exponentially with a decay length of 0.7 nm for dioleoylphosphatidylcholine, 1.2 nm for dioleoylphosphatidylserine, and 0.8 nm for dioleoyloxypropyl trimethylammonium chloride. The salt concentration drastically changed the interaction between dioleoyloxypropyl trimethylammonium chloride bilayers. As an example for the influence of proteins on bilayer-bilayer interaction, the influence of the synaptic vesicle-associated, phospholipid binding protein synapsin I was studied. Synapsin I increased membrane stability so that the bilayers could not be penetrated with the tip.

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AdsorptionElasticityLipid BilayersLiposomesMacromolecular SubstancesMembrane FluidityMembrane FusionMembranes, ArtificialMicromanipulationMicroscopy, Atomic ForcePhospholipidsProtein BindingStress, MechanicalSynapsinsEvaluation StudyJournal ArticleResearch Support, Non-U.S. Gov't

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Ioana Pera, Rüdiger Stark, Michael Kappl, Hans-Jürgen Butt, Fabio Benfenati. 2004. Using the atomic force microscope to study the interaction between two solid supported lipid bilayers and the influence of synapsin I.. https://doi.org/10.1529/biophysj.104.044214

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