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Probing the Self-Assembly and the Accompanying Structural Changes of Hydrophobin SC3 on a Hydrophobic Surface by Mass Spectrometry

X. Wang ^*, H. P. Permentier , R. Rink , J. A. W. Kruijtzer , R. M. J. Liskamp , H. A. B. Wösten ^¶, B. Poolman ^* and G. T. Robillard ^* 

^* Department of Biochemistry and Mass Spectrometry Core Facility, University of Groningen, Groningen, The Netherlands; Biomade Technology Foundation, Groningen, The Netherlands; and Department of Medicinal Chemistry and ^¶ Department of Microbiology, Institute of Biomembranes, University of Utrecht, Utrecht, The Netherlands

Correspondence: Address reprint requests to G. T. Robillard, BioMaDe Technology, Nijenborgh 4, 9747 AG Groningen, The Netherlands. Tel.: 031-50-3634321; Fax: 031-50-3634429; E-mail: robillard{at}biomade.nl.

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 -helical state to the stable end form called the ß-sheet state. Self-assembly of the hydrophobin at the Teflon surface is arrested in the -helical state. The ß-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 -helical structure and resulted in low solvent accessibility. The solvent-protected region of the second loop extended upon conversion to the ß-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.

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				X. Wang, F. Shi, H. A. B. Wosten, H. Hektor, B. Poolman, and G. T. Robillard The SC3 Hydrophobin Self-Assembles into a Membrane with Distinct Mass Transfer Properties Biophys. J., May 1, 2005; 88(5): 3434 - 3443. [Abstract] [Full Text] [PDF]