Self-Assembly and Conformational Changes of Hydrophobin Classes at the Air-Water Interface

Konrad Meister (Corresponding Author), Alexander Bäumer, Géza R. Szilvay, Arja Paananen, Huib J. Bakker

    Research output: Contribution to journalArticleScientificpeer-review

    24 Citations (Scopus)


    We use surface-specific vibrational sum-frequency generation spectroscopy (VSFG) to study the structure and self-assembling mechanism of the class I hydrophobin SC3 from Schizophyllum commune and the class II hydrophobin HFBI from Trichoderma reesei. We find that both hydrophobins readily accumulate at the water–air interface and form rigid, highly ordered protein films that give rise to prominent VSFG signals. We identify several resonances that are associated with β-sheet structures and assign them to the central β-barrel core present in both proteins. Differences between the hydrophobin classes are observed in their interfacial self-assembly. For HFBI, we observe no changes in conformation upon adsorption to the water surface. For SC3, we observe an increase in β-sheet-specific signals that supports a surface-driven self-assembly mechanism in which the central β-barrel remains intact and stacks into a larger-scale architecture, amyloid-like rodlets.
    Original languageEnglish
    Pages (from-to)4067-4071
    JournalThe Journal of Physical Chemistry Letters
    Issue number20
    Publication statusPublished - 2016
    MoE publication typeA1 Journal article-refereed


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