REVERSED MICELLAR APPROACH AS A NEW TOOL FOR THE FORMATION AND STRUCTURAL STUDIES OF PROTEIN LANGMUIR-BLODGETT-FILMS

Reversed micelles of sodium diisooctylsulfosuccinate with cytochrome c were used as spreading solutions for Langmuir-Blodgett film formation. A condensed monolayer with closely packed surfactant molecules in the air and closely packed protein molecules under the water surface was formed after several repetitions of the compression-expansion cycle. The resulting film was transferred onto the solid substrate. The films were studied by circular dichroism and by small-angle X-ray scattering. It was shown that the metalloprotein in the film is not denatured and the resulting thin film is significantly ordered, more so than the corresponding monocomponent protein Langmuir-Blodgett films.