Abstract
Hydrophobins are small fungal proteins, which have remarkable surface–chemical properties. They self-assemble at hydrophobic/hydrophilic interfaces and work as adhesive agents and coatings. Sixteen layer Langmuir–Blodgett films of hydrophobins HFBI and HFBII from the fungus Trichoderma reesei were prepared and studied using grazing-incidence X-ray diffraction and reflectivity techniques. Both kind of films contain hexagonally ordered crystallites on the substrate with unit cell parameters of a = b = 54 Å (HFBI) and a = b = 55 Å (HFBII). The structure is similar to the structure of monolayer Langmuir–Blodgett films.
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