Self-assembly of class II hydrophobins on highly polar surfaces
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Hydrophobins, adhesive proteins produced by filamentous fungi, have been described as the most surface active proteins known and show extraordinary properties regarding formation of surfaces. Hydrophobins have roles in the growth and development of the fungi including function in adhesion to surfaces, reducing surface tension for aerial growth and spore hydrophobicity and to aid spreading of aerial spores. Observations of filamentous fungi show that the structures formed by their mycelia can be very hydrophobic. Furthermore, airborne spores (conidia) covered with a surface layer of hydrophobin has been shown to mask the recognition of the conidia by the human immune system and hence prevents immune response. The knowledge of how hydrophobins aid in producing these fascinating properties is far from complete. This study a
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