Abstract

Tethered lipid bilayers were formed on oxidized Si surfaces using the avidin–biotin interaction to investigate the lipid–membrane protein interactions by using gramicidin-A (g-A) as a model membrane protein. The morphology of the tethered lipid bilayer, observed by in situ atomic force microscopy (AFM), changed drastically by the reconstruction of g-A. The aggregation behavior of g-A was clearly different in the tethered membrane from those in simple supported membranes on mica and SiO 2 surfaces.

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