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Self-assembly of class II hydrophobins on polar surfaces

Journal article
Authors Mathias S. Grunér
Géza R. Szilvay
Mattias Berglin
Michael Lienemann
Päivi Laaksonen
Markus B. Linder
Published in Langmuir
Volume 28
Pages 4293-4300
ISSN 07437463
Publication year 2012
Published at Department of Chemistry and Molecular Biology
Pages 4293-4300
Language en
Subject categories Biological Sciences


Hydrophobins are structural proteins produced by filamentous fungi that are amphiphilic and function through self-assembling into structures such as membranes. They have diverse roles in the growth and development of fungi, for example in adhesion to substrates, for reducing surface tension to allow aerial growth, in forming protective coatings on spores and other structures. Hydrophobin membranes at the air-water interface and on hydrophobic solids are well studied, but understanding how hydrophobins can bind to a polar surface to make it more hydrophobic has remained unresolved. Here we have studied different class II hydrophobins for their ability to bind to polar surfaces that were immersed in buffer solution. We show here that the binding under some conditions results in a significant increase of water contact angle (WCA) on some surfaces. The highest contact angles were obtained on cationic surfaces where the hydrophobin HFBI has an average WCA of 62.6° at pH 9.0, HFBII an average of 69.0° at pH 8.0, and HFBIII had an average WCA of 61.9° at pH 8.0. The binding of the hydrophobins to the positively charged surface was shown to depend on both pH and ionic strength. The results are significant for understanding the mechanism for formation of structures such as the surface of mycelia or fungal spore coatings as well as for possible technical applications. © 2012 American Chemical Society.

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