Modification of interfacial forces by hydrophobin HFBI

Irit Goldian, Sabrina Jahn, Päivi Laaksonen, Markus Linder, Nir Kampf, Jacob Klein (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

8 Citations (Scopus)

Abstract

Using a surface force balance, we have measured the forces between bare (hydrophilic) mica surfaces, and between hydrophobized mica surfaces, in each case coated with the amphiphilic protein hydrophobin (HFBI) from Trichoderma reesei. We additionally characterized these surfaces by contact angle measurements and AFM. The results are consistent with the formation of hydrophobic surfaces exposed by HFBI adsorbed on the hydrophilic substrate, and hydrophilic surfaces exposed by HFBI adsorbed on the hydrophobic substrate. In particular, friction between HFBI surfaces on hydrophobized mica, exposing hydrophilic surfaces, is an order of magnitude lower than friction between HFBI-coated hydrophilic surfaces, which expose the hydrophobic side of the protein to the water interface. This result can be readily understood in terms of the greater hydration level of the exposed outer surfaces in the former case.
Original languageEnglish
Pages (from-to)10627-10639
JournalSoft Matter
Volume9
Issue number44
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fingerprint

mica
friction
1-(heptafluorobutyryl)imidazole
Friction
proteins
Substrates
Angle measurement
Hydration
Contact angle
hydration
Proteins
atomic force microscopy
Water
water

Cite this

Goldian, I., Jahn, S., Laaksonen, P., Linder, M., Kampf, N., & Klein, J. (2013). Modification of interfacial forces by hydrophobin HFBI. Soft Matter, 9(44), 10627-10639. https://doi.org/10.1039/C3SM51924D
Goldian, Irit ; Jahn, Sabrina ; Laaksonen, Päivi ; Linder, Markus ; Kampf, Nir ; Klein, Jacob. / Modification of interfacial forces by hydrophobin HFBI. In: Soft Matter. 2013 ; Vol. 9, No. 44. pp. 10627-10639.
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abstract = "Using a surface force balance, we have measured the forces between bare (hydrophilic) mica surfaces, and between hydrophobized mica surfaces, in each case coated with the amphiphilic protein hydrophobin (HFBI) from Trichoderma reesei. We additionally characterized these surfaces by contact angle measurements and AFM. The results are consistent with the formation of hydrophobic surfaces exposed by HFBI adsorbed on the hydrophilic substrate, and hydrophilic surfaces exposed by HFBI adsorbed on the hydrophobic substrate. In particular, friction between HFBI surfaces on hydrophobized mica, exposing hydrophilic surfaces, is an order of magnitude lower than friction between HFBI-coated hydrophilic surfaces, which expose the hydrophobic side of the protein to the water interface. This result can be readily understood in terms of the greater hydration level of the exposed outer surfaces in the former case.",
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Goldian, I, Jahn, S, Laaksonen, P, Linder, M, Kampf, N & Klein, J 2013, 'Modification of interfacial forces by hydrophobin HFBI', Soft Matter, vol. 9, no. 44, pp. 10627-10639. https://doi.org/10.1039/C3SM51924D

Modification of interfacial forces by hydrophobin HFBI. / Goldian, Irit; Jahn, Sabrina; Laaksonen, Päivi; Linder, Markus; Kampf, Nir; Klein, Jacob (Corresponding Author).

In: Soft Matter, Vol. 9, No. 44, 2013, p. 10627-10639.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Modification of interfacial forces by hydrophobin HFBI

AU - Goldian, Irit

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AU - Laaksonen, Päivi

AU - Linder, Markus

AU - Kampf, Nir

AU - Klein, Jacob

PY - 2013

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N2 - Using a surface force balance, we have measured the forces between bare (hydrophilic) mica surfaces, and between hydrophobized mica surfaces, in each case coated with the amphiphilic protein hydrophobin (HFBI) from Trichoderma reesei. We additionally characterized these surfaces by contact angle measurements and AFM. The results are consistent with the formation of hydrophobic surfaces exposed by HFBI adsorbed on the hydrophilic substrate, and hydrophilic surfaces exposed by HFBI adsorbed on the hydrophobic substrate. In particular, friction between HFBI surfaces on hydrophobized mica, exposing hydrophilic surfaces, is an order of magnitude lower than friction between HFBI-coated hydrophilic surfaces, which expose the hydrophobic side of the protein to the water interface. This result can be readily understood in terms of the greater hydration level of the exposed outer surfaces in the former case.

AB - Using a surface force balance, we have measured the forces between bare (hydrophilic) mica surfaces, and between hydrophobized mica surfaces, in each case coated with the amphiphilic protein hydrophobin (HFBI) from Trichoderma reesei. We additionally characterized these surfaces by contact angle measurements and AFM. The results are consistent with the formation of hydrophobic surfaces exposed by HFBI adsorbed on the hydrophilic substrate, and hydrophilic surfaces exposed by HFBI adsorbed on the hydrophobic substrate. In particular, friction between HFBI surfaces on hydrophobized mica, exposing hydrophilic surfaces, is an order of magnitude lower than friction between HFBI-coated hydrophilic surfaces, which expose the hydrophobic side of the protein to the water interface. This result can be readily understood in terms of the greater hydration level of the exposed outer surfaces in the former case.

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DO - 10.1039/C3SM51924D

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JO - Soft Matter

JF - Soft Matter

SN - 1744-683X

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Goldian I, Jahn S, Laaksonen P, Linder M, Kampf N, Klein J. Modification of interfacial forces by hydrophobin HFBI. Soft Matter. 2013;9(44):10627-10639. https://doi.org/10.1039/C3SM51924D