Hydrophobins are a group of highly surface active, self-assembling fungal proteins. They function as coatings on various fungal structures, work as adhesive agents, and enable aerial growth of hyphae . In this work we have focussed on two class II hydrophobins from Trichoderma reesei, HFBI and HFBII . Langmuir-Blodgett films of HFBI and HFBII analysed by atomic force microscopy (AFM) showed highly organised two-dimensional crystalline structures for both hydrophobins . Comparison between AFM data of ordered films and small-angle X-ray scattering results of hydrophobin solutions  indicated that the unit cells in the films have dimensions similar to those of tetrameric aggregates found in solutions. Moreover, these hydrophobins form nanostructured films at air-water interface spontaneously . This detailed structural study of hydrophobin films brings the interest in new options for surface modification and nanostructured materials.
|Publication status||Published - 2006|
|MoE publication type||Not Eligible|
|Event||VIII Linz Winter Workshop: Advances in Single Molecule Research for Biology and Nanoscience - Linz, Austria|
Duration: 3 Feb 2006 → 6 Feb 2006
|Conference||VIII Linz Winter Workshop|
|Period||3/02/06 → 6/02/06|