Probing the self-assembly and the accompanying structural changes of hydrophobin SC3 on a hydrophobic surface by mass spectrometry

Wang, X., Permentier, H.P., Rink, R., Kruijtzer, J.A.W., Liskamp, R.M.J. , Wösten, H.A.B., Poolman, B. and Robillard, G.T. (2004) Probing the self-assembly and the accompanying structural changes of hydrophobin SC3 on a hydrophobic surface by mass spectrometry. Biophysical Journal, 87(3), pp. 1919-1928. (doi:10.1529/biophysj.104.041616)

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Abstract

The fungal class I hydrophobin SC3 self-assembles into an amphipathic membrane at hydrophilic-hydrophobic interfaces such as the water-air and water-Teflon interface. During self-assembly, the water-soluble state of SC3 proceeds via the intermediate α-helical state to the stable end form called the β-sheet state. Self-assembly of the hydrophobin at the Teflon surface is arrested in the α-helical state. The β-sheet state can be induced at elevated temperature in the presence of detergent. The structural changes of SC3 were monitored by various mass spectrometry techniques. We show that the so-called second loop of SC3 (C39–S72) has a high affinity for Teflon. Binding of this part of SC3 to Teflon was accompanied by the formation of α-helical structure and resulted in low solvent accessibility. The solvent-protected region of the second loop extended upon conversion to the β-sheet state. In contrast, the C-terminal part of SC3 became more exposed to the solvent. The results indicate that the second loop of class I hydrophobins plays a pivotal role in self-assembly at the hydrophilic-hydrophobic interface. Of interest, this loop is much smaller in case of class II hydrophobins, which may explain the differences in their assembly.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Wang, X., Permentier, H.P., Rink, R., Kruijtzer, J.A.W., Liskamp, R.M.J., Wösten, H.A.B., Poolman, B., and Robillard, G.T.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Biophysical Journal
ISSN:0006-3495
ISSN (Online):1542-0086

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