Self-assembled films of hydrophobin proteins HFBI and HFBII studied in situ at the air/water interface

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

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Hydrophobins are a group of surface-active fungal proteins known to adsorb to the air/water interface and self-assemble into highly crystalline films. We characterized the self-assembled protein films of two hydrophobins, HFBI and HFBII from Trichoderma reesei, directly at the air/water interface using Brewster angle microscopy, grazing-incidence X-ray diffraction, and reflectivity. Already in zero surface pressure, HFBI and HFBII self-assembled into micrometer-sized rafts containing hexagonally ordered two-dimensional crystallites with lattice constants of 55 Å and 56 Å, respectively. Increasing the pressure did not change the ordering of the proteins in the crystallites. According to the reflectivity measurements, the thicknesses of the hydrophobin films were 28 Å (HFBI) and 24 Å (HFBII) at 20 mN/m. The stable films could also be transferred to a silicon substrate. Modeling of the diffraction data indicated that both hydrophobin films contained six molecules in the unit cell, but the ordering of the molecules was somewhat different for HFBI and HFBII, suggesting specific protein−protein interactions.
Original languageEnglish
Pages (from-to)1612-1619
Number of pages8
JournalLangmuir
Volume25
Issue number3
DOIs
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed

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proteins
Proteins
Water
air
Air
water
Crystallites
crystallites
reflectance
rafts
Molecules
Fungal Proteins
Brewster angle
Silicon
grazing incidence
diffraction
Lattice constants
micrometers
molecules
Microscopic examination

Cite this

Kisko, K., Szilvay, G., Vuorimaa, E., Lemmetyinen, H., Linder, M., Torkkeli, M., & Serimaa, R. (2009). Self-assembled films of hydrophobin proteins HFBI and HFBII studied in situ at the air/water interface. Langmuir, 25(3), 1612-1619. https://doi.org/10.1021/la803252g
Kisko, Kaisa ; Szilvay, Geza ; Vuorimaa, Elina ; Lemmetyinen, Helge ; Linder, Markus ; Torkkeli, Mika ; Serimaa, Ritva. / Self-assembled films of hydrophobin proteins HFBI and HFBII studied in situ at the air/water interface. In: Langmuir. 2009 ; Vol. 25, No. 3. pp. 1612-1619.
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abstract = "Hydrophobins are a group of surface-active fungal proteins known to adsorb to the air/water interface and self-assemble into highly crystalline films. We characterized the self-assembled protein films of two hydrophobins, HFBI and HFBII from Trichoderma reesei, directly at the air/water interface using Brewster angle microscopy, grazing-incidence X-ray diffraction, and reflectivity. Already in zero surface pressure, HFBI and HFBII self-assembled into micrometer-sized rafts containing hexagonally ordered two-dimensional crystallites with lattice constants of 55 {\AA} and 56 {\AA}, respectively. Increasing the pressure did not change the ordering of the proteins in the crystallites. According to the reflectivity measurements, the thicknesses of the hydrophobin films were 28 {\AA} (HFBI) and 24 {\AA} (HFBII) at 20 mN/m. The stable films could also be transferred to a silicon substrate. Modeling of the diffraction data indicated that both hydrophobin films contained six molecules in the unit cell, but the ordering of the molecules was somewhat different for HFBI and HFBII, suggesting specific protein−protein interactions.",
author = "Kaisa Kisko and Geza Szilvay and Elina Vuorimaa and Helge Lemmetyinen and Markus Linder and Mika Torkkeli and Ritva Serimaa",
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Kisko, K, Szilvay, G, Vuorimaa, E, Lemmetyinen, H, Linder, M, Torkkeli, M & Serimaa, R 2009, 'Self-assembled films of hydrophobin proteins HFBI and HFBII studied in situ at the air/water interface', Langmuir, vol. 25, no. 3, pp. 1612-1619. https://doi.org/10.1021/la803252g

Self-assembled films of hydrophobin proteins HFBI and HFBII studied in situ at the air/water interface. / Kisko, Kaisa (Corresponding Author); Szilvay, Geza; Vuorimaa, Elina; Lemmetyinen, Helge; Linder, Markus; Torkkeli, Mika; Serimaa, Ritva.

In: Langmuir, Vol. 25, No. 3, 2009, p. 1612-1619.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Self-assembled films of hydrophobin proteins HFBI and HFBII studied in situ at the air/water interface

AU - Kisko, Kaisa

AU - Szilvay, Geza

AU - Vuorimaa, Elina

AU - Lemmetyinen, Helge

AU - Linder, Markus

AU - Torkkeli, Mika

AU - Serimaa, Ritva

PY - 2009

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N2 - Hydrophobins are a group of surface-active fungal proteins known to adsorb to the air/water interface and self-assemble into highly crystalline films. We characterized the self-assembled protein films of two hydrophobins, HFBI and HFBII from Trichoderma reesei, directly at the air/water interface using Brewster angle microscopy, grazing-incidence X-ray diffraction, and reflectivity. Already in zero surface pressure, HFBI and HFBII self-assembled into micrometer-sized rafts containing hexagonally ordered two-dimensional crystallites with lattice constants of 55 Å and 56 Å, respectively. Increasing the pressure did not change the ordering of the proteins in the crystallites. According to the reflectivity measurements, the thicknesses of the hydrophobin films were 28 Å (HFBI) and 24 Å (HFBII) at 20 mN/m. The stable films could also be transferred to a silicon substrate. Modeling of the diffraction data indicated that both hydrophobin films contained six molecules in the unit cell, but the ordering of the molecules was somewhat different for HFBI and HFBII, suggesting specific protein−protein interactions.

AB - Hydrophobins are a group of surface-active fungal proteins known to adsorb to the air/water interface and self-assemble into highly crystalline films. We characterized the self-assembled protein films of two hydrophobins, HFBI and HFBII from Trichoderma reesei, directly at the air/water interface using Brewster angle microscopy, grazing-incidence X-ray diffraction, and reflectivity. Already in zero surface pressure, HFBI and HFBII self-assembled into micrometer-sized rafts containing hexagonally ordered two-dimensional crystallites with lattice constants of 55 Å and 56 Å, respectively. Increasing the pressure did not change the ordering of the proteins in the crystallites. According to the reflectivity measurements, the thicknesses of the hydrophobin films were 28 Å (HFBI) and 24 Å (HFBII) at 20 mN/m. The stable films could also be transferred to a silicon substrate. Modeling of the diffraction data indicated that both hydrophobin films contained six molecules in the unit cell, but the ordering of the molecules was somewhat different for HFBI and HFBII, suggesting specific protein−protein interactions.

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DO - 10.1021/la803252g

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