Interactions of hydrophobin proteins in solution studied by small-angle x-ray scattering

Kaisa Kisko (Corresponding Author), Géza Szilvay, Ulla Vainio, Markus Linder, Ritva Serimaa

Research output: Contribution to journalArticleScientificpeer-review

41 Citations (Scopus)

Abstract

Hydrophobins are a group of very surface-active, fungal proteins known to self-assemble on various hydrophobic/hydrophilic interfaces. The self-assembled films coat fungal structures and mediate their attachment to surfaces. Hydrophobins are also soluble in water. Here, the association of hydrophobins HFBI and HFBII from Trichoderma reesei in aqueous solution was studied using small-angle x-ray scattering. Both HFBI and HFBII exist mainly as tetramers in solution in the concentration range 0.5–10 mg/ml. The assemblies of HFBII dissociate more easily than those of HFBI, which can tolerate changes of pH from 3 to 9 and temperatures in the range 5°C–60°C. The self-association of HFBI and HFBII is mainly driven by the hydrophobic effect, and addition of salts along the Hofmeister series promotes the formation of larger assemblies, whereas ethanol breaks the tetramers into monomers. The possibility that the oligomers in solution form the building blocks of the self-assembled film at the air/water interface is discussed.
Original languageEnglish
Pages (from-to)198-206
JournalBiophysical Journal
Volume94
Issue number1
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

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X-Rays
Proteins
Fungal Structures
Trichoderma
Fungal Proteins
Water
Ethanol
Salts
Air
Temperature
1-(heptafluorobutyryl)imidazole

Cite this

Kisko, Kaisa ; Szilvay, Géza ; Vainio, Ulla ; Linder, Markus ; Serimaa, Ritva. / Interactions of hydrophobin proteins in solution studied by small-angle x-ray scattering. In: Biophysical Journal. 2008 ; Vol. 94, No. 1. pp. 198-206.
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abstract = "Hydrophobins are a group of very surface-active, fungal proteins known to self-assemble on various hydrophobic/hydrophilic interfaces. The self-assembled films coat fungal structures and mediate their attachment to surfaces. Hydrophobins are also soluble in water. Here, the association of hydrophobins HFBI and HFBII from Trichoderma reesei in aqueous solution was studied using small-angle x-ray scattering. Both HFBI and HFBII exist mainly as tetramers in solution in the concentration range 0.5–10 mg/ml. The assemblies of HFBII dissociate more easily than those of HFBI, which can tolerate changes of pH from 3 to 9 and temperatures in the range 5°C–60°C. The self-association of HFBI and HFBII is mainly driven by the hydrophobic effect, and addition of salts along the Hofmeister series promotes the formation of larger assemblies, whereas ethanol breaks the tetramers into monomers. The possibility that the oligomers in solution form the building blocks of the self-assembled film at the air/water interface is discussed.",
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Interactions of hydrophobin proteins in solution studied by small-angle x-ray scattering. / Kisko, Kaisa (Corresponding Author); Szilvay, Géza; Vainio, Ulla; Linder, Markus; Serimaa, Ritva.

In: Biophysical Journal, Vol. 94, No. 1, 2008, p. 198-206.

Research output: Contribution to journalArticleScientificpeer-review

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AB - Hydrophobins are a group of very surface-active, fungal proteins known to self-assemble on various hydrophobic/hydrophilic interfaces. The self-assembled films coat fungal structures and mediate their attachment to surfaces. Hydrophobins are also soluble in water. Here, the association of hydrophobins HFBI and HFBII from Trichoderma reesei in aqueous solution was studied using small-angle x-ray scattering. Both HFBI and HFBII exist mainly as tetramers in solution in the concentration range 0.5–10 mg/ml. The assemblies of HFBII dissociate more easily than those of HFBI, which can tolerate changes of pH from 3 to 9 and temperatures in the range 5°C–60°C. The self-association of HFBI and HFBII is mainly driven by the hydrophobic effect, and addition of salts along the Hofmeister series promotes the formation of larger assemblies, whereas ethanol breaks the tetramers into monomers. The possibility that the oligomers in solution form the building blocks of the self-assembled film at the air/water interface is discussed.

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