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Biophysical Journal 87:2446-2455 (2004)
© 2004 The Biophysical Society

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 * and Fabio Benfenati {dagger}

* Max-Planck-Institute for Polymer Research, D-55128 Mainz, Germany; and {dagger} Department of Experimental Medicine, Section of Human Physiology, University of Genoa, 16132 Genoa, Italy

Correspondence: Address reprint requests to Hans-Jürgen Butt, Tel.: 49-6131-379 111; Fax: 149-6131-379 310; E-mail: butt{at}mpip-mainz.mpg.de.

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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