Mechanisms of protein adhesion on surface films of hydrophobin

Zefang Wang, Michael Lienemann, Mingqiang Qiau, Markus Linder

Research output: Contribution to journalArticleScientificpeer-review

58 Citations (Scopus)

Abstract

Hydrophobins are adhesive proteins produced by filamentous fungi. They are in many cases secreted into the medium and adsorb readily to a number of different surfaces. They fulfill many different tasks such as the formation of various coatings and mediating adhesion of fungi to surfaces. The mechanism of how hydrophobins adhere and how they mediate fungal adhesion is of interest both from the point of view of fungal biology and for various biotechnical immobilization applications. It has been shown that hydrophobins typically form a monomolecular layer on solid substrates. We are especially interested in how a surface layer of hydrophobin can mediate the adhesion of a second layer of another protein. In this work we systematically studied how proteins adsorb onto hydrophobins that are bound as monomolecular layers on nonpolar surfaces. We found that several types of proteins readily adsorb onto hydrophobins, but only under defined conditions of pH and ionic strength. The binding conditions were also highly dependent on the adhering protein. By studying solution conditions such as pH and ionic strength, we conclude that the surface adhesion is due to selective Coulombic charge interactions. We conclude that hydrophobins can transform a nonpolar surface into one that efficiently recruits other proteins by charge interactions.
Original languageEnglish
Pages (from-to)8491 - 8496
JournalLangmuir
Volume26
Issue number11
DOIs
Publication statusPublished - 3 May 2010
MoE publication typeA1 Journal article-refereed

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adhesion
Adhesion
proteins
Proteins
fungi
Ionic strength
Fungi
Monolayers
immobilization
biology
adhesives
Adhesives
surface layers
interactions
coatings
Coatings
Substrates

Cite this

Wang, Zefang ; Lienemann, Michael ; Qiau, Mingqiang ; Linder, Markus. / Mechanisms of protein adhesion on surface films of hydrophobin. In: Langmuir. 2010 ; Vol. 26, No. 11. pp. 8491 - 8496.
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Mechanisms of protein adhesion on surface films of hydrophobin. / Wang, Zefang; Lienemann, Michael; Qiau, Mingqiang; Linder, Markus.

In: Langmuir, Vol. 26, No. 11, 03.05.2010, p. 8491 - 8496.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Mechanisms of protein adhesion on surface films of hydrophobin

AU - Wang, Zefang

AU - Lienemann, Michael

AU - Qiau, Mingqiang

AU - Linder, Markus

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Y1 - 2010/5/3

N2 - Hydrophobins are adhesive proteins produced by filamentous fungi. They are in many cases secreted into the medium and adsorb readily to a number of different surfaces. They fulfill many different tasks such as the formation of various coatings and mediating adhesion of fungi to surfaces. The mechanism of how hydrophobins adhere and how they mediate fungal adhesion is of interest both from the point of view of fungal biology and for various biotechnical immobilization applications. It has been shown that hydrophobins typically form a monomolecular layer on solid substrates. We are especially interested in how a surface layer of hydrophobin can mediate the adhesion of a second layer of another protein. In this work we systematically studied how proteins adsorb onto hydrophobins that are bound as monomolecular layers on nonpolar surfaces. We found that several types of proteins readily adsorb onto hydrophobins, but only under defined conditions of pH and ionic strength. The binding conditions were also highly dependent on the adhering protein. By studying solution conditions such as pH and ionic strength, we conclude that the surface adhesion is due to selective Coulombic charge interactions. We conclude that hydrophobins can transform a nonpolar surface into one that efficiently recruits other proteins by charge interactions.

AB - Hydrophobins are adhesive proteins produced by filamentous fungi. They are in many cases secreted into the medium and adsorb readily to a number of different surfaces. They fulfill many different tasks such as the formation of various coatings and mediating adhesion of fungi to surfaces. The mechanism of how hydrophobins adhere and how they mediate fungal adhesion is of interest both from the point of view of fungal biology and for various biotechnical immobilization applications. It has been shown that hydrophobins typically form a monomolecular layer on solid substrates. We are especially interested in how a surface layer of hydrophobin can mediate the adhesion of a second layer of another protein. In this work we systematically studied how proteins adsorb onto hydrophobins that are bound as monomolecular layers on nonpolar surfaces. We found that several types of proteins readily adsorb onto hydrophobins, but only under defined conditions of pH and ionic strength. The binding conditions were also highly dependent on the adhering protein. By studying solution conditions such as pH and ionic strength, we conclude that the surface adhesion is due to selective Coulombic charge interactions. We conclude that hydrophobins can transform a nonpolar surface into one that efficiently recruits other proteins by charge interactions.

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