Abstract
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 [1]. In this work we have focussed on two class II hydrophobins from Trichoderma reesei, HFBI and HFBII [2]. Langmuir-Blodgett films of HFBI and HFBII analysed by atomic force microscopy (AFM) showed highly organised two-dimensional crystalline structures for both hydrophobins [3]. Comparison between AFM data of ordered films and small-angle X-ray scattering results of hydrophobin solutions [4] 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 [5]. This detailed structural study of hydrophobin films brings the interest in new options for surface modification and nanostructured materials.
| Original language | English |
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| 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
| Conference | VIII Linz Winter Workshop |
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| Country/Territory | Austria |
| City | Linz |
| Period | 3/02/06 → 6/02/06 |