The PM IRRAS is applied for structural analysis of bilayers of 1,2dimyristoyl-sn-glycero-3-phosphocholine (DMPC) deposited using the Langmuir-Blodgett and Langmuir-Schaefer techniques on gold, silica and titania surfaces. Lipid films formed on Au, Au|SiO₂ and Au|Ti|TiO₂ surfaces show two-dimensional long range order. The hydrocarbon chains exist in a liquid and a gel phase, depending on the surface pressure of the film transfer. Interactions between positively charged choline and the negatively charged silica and titania surfaces influence the arrangement of the polar head group of the lipid molecule at the interface. On the titania surface in a loosely packed bilayer the polar head group has an open conformation. In a densely packed bilayer on all surfaces interactions between the choline and phosphate groups of DMPC predominate interactions with the surface, changing the conformation of the polar head group.

A lipid bilayer exposed to the electric field mimics a natural cell membrane. The lipid bilayer assembled on the gold electrode was exposed to protein solutions interacting specifically either with a glycolipid or with a phospholipid. Charge accumulated on the membrane, capacity, potential window of film adsorption were determined electrochemically.

A successful adaptation of an implant material in an organism is governed by the adsorption processes of the extracellular matrix. The great success of titania implants is connected with a formation of collagen rich layer on its surface. The process of adsorption of collagen helices on the Au|Ti|TiO₂ surface was monitored by the PM IRRAS. In an electrolyte solution, however, a collagen coating is unstable. A significant improvement of the stability of the collagen layer was obtained, when the protein was coadsorbed with a polysaccharide (heparine) on the surface of titania pre-treated in 20 mM CaCl₂ solution. The PM IRRA spectra of collagen on the titania surface show a blue-shift of the amide I band, as compared to an IR spectrum in aqueous solution. The collagen helix is less hydrated / weaker hydrogen bonded in the adsorbed state, indicating that a hydrogen bonding network in the triple helix of collagen changes upon adsorption.

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