The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reesei

Hydrophobins are small fungal surface active proteins that self-assemble at interfaces into films with nanoscale structures. The hydrophobin HFBI from Trichoderma reesei has been shown to associate in solution into tetramers but the role of this association on the function of HFBI has remained uncle...

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Bibliographic Details
Published in:FEBS letters 2007-06, Vol.581 (14), p.2721-2726
Main Authors: Szilvay, Géza R., Kisko, Kaisa, Serimaa, Ritva, Linder, Markus B.
Format: Article
Language:English
Subjects:
Adsorption
Amino Acid Sequence
Ascomycota - chemistry
Ascomycota - genetics
Chromatography, Gel
Crystallography, X-Ray
Dimerization
dithiothreitol
DTT
Fungal Proteins - chemistry
Fungal Proteins - genetics
Fungal Proteins - isolation & purification
Hydrophobic and Hydrophilic Interactions
Hydrophobin
Hypocrea jecorina
Molecular Sequence Data
Polymers - chemistry
Protein Conformation
Protein multimerization
Protein self-assembly
QCM
quartz crystal microbalance
SAXS
SEC
Sequence Homology, Amino Acid
size exclusion chromatography
small angle X-ray scattering
Solutions - chemistry
Surface active protein
Surface Properties
Thermodynamics
Water - chemistry
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Summary:Hydrophobins are small fungal surface active proteins that self-assemble at interfaces into films with nanoscale structures. The hydrophobin HFBI from Trichoderma reesei has been shown to associate in solution into tetramers but the role of this association on the function of HFBI has remained unclear. We produced two HFBI variants that showed a significant shift in solution association equilibrium towards the tetramer state. However, this enhanced solution association did not alter the surface properties of the variant HFBIs. The results show that there is not a strong relationship between HFBI solution association state and surface properties such as surface activity.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.05.024