Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei

Kaisa Kisko (Corresponding Author), Géza Szilvay, Elina Vuorimaa, Helge Lemmetyinen, Markus Linder, Mika Torkkeli, Ritva Serimaa

    Research output: Contribution to journalArticleScientificpeer-review

    16 Citations (Scopus)


    Hydrophobins are a group of small amphiphilic proteins which are known to self-assemble on interfaces.
    They contain eight conserved cysteine residues, which make four disulfide bridges. A new hydrophobin protein, HFBIII, from the fungus Trichoderma reesei contains one extra cysteine residue, giving the protein a naturally reactive site.
    The self-assembly of hydrophobin protein HFBIII was studied using grazing-incidence X-ray diffraction and reflectivity. HFBIII self-assembles into a hexagonally ordered monolayer at an air/water interface and also forms crystalline coatings on a silicon substrate. The lattice constants for the hexagonal coatings are a = b = 56.5 Å, [gamma] = 120°.
    The self-assembled structure in the HFBIII film is very similar to those formed by two other T. reesei hydrophobins, HFBI and HFBII.
    Original languageEnglish
    Pages (from-to)s355-s360
    JournalJournal of Applied Crystallography
    Issue numberPart s1
    Publication statusPublished - 2007
    MoE publication typeA1 Journal article-refereed


    • hydrophobins
    • grazing-incidence X-ray diffraction
    • self-assembly
    • reflectivity


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