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Thesis: Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei
31.10.2007
Géza R Szilvay, Research Scientist from VTT’s Nanobiomaterials Team presents his dissertation “Self-assembly of hydrophobin proteins from the fungus Trichoderma reesei” on 2 November 2007 at 12 in the University of Helsinki (Viikinkaari 5, Helsinki).
Hydrophobins are small surface active proteins that are produced by
filamentous fungi. The surface activity of hydrophobin proteins leads to the
formation of a film at the air-water interface and adsorption to surfaces. The
formation of these hydrophobin films and coatings is important in many stages
of fungal development. Furthermore, these properties make hydrophobins
interesting for potential use in technical applications for example as
components in diagnostic kits or sensors. The self-assembling properties of
hydrophobins could be utilized in nanotechnological applications where
structural control at the molecular scale is needed.
The
surfactant-like properties of hydrophobins from Trichoderma reesei were
studied at the air-water interface, at solid surfaces, and in solution. The
hydrophobin HFBI was observed to spontaneously form a cohesive film on a water
drop. The film was imaged using atomic force microscopy from both sides,
revealing a monomolecular film with a defined molecular structure.
The
use of hydrophobins as surface immobilization carriers for enzymes was studied
using fusion proteins of HFBI or HFBII and an enzyme. Furthermore,
site-specifically modified variants of HFBI were shown to retain their ability
to self-assemble at interfaces and to be able to bind a second layer of
proteins by biomolecular recognition.
In order to understand
the function of hydrophobins at interfaces, an understanding of their overall
behaviour and self-assembly is needed. HFBI and HFBII were shown to associate
in solution into dimers and tetramers in a concentration-dependent manner. The
association dynamics and protein-protein interactions of HFBI and HFBII were
studied using Förster resonance energy transfer and size exclusion
chromatography. It was shown that the surface activity of HFBI is not directly
dependent on the formation of multimers in solution.
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