The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII

Research output: Contribution to journalArticle

Standard

The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII. / Grunér, M.S.; Paananen, A.; Szilvay, Géza R.; Linder, M. B.

In: Colloids and Surfaces B: Biointerfaces, Vol. 155, 01.07.2017, p. 111-117.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Bibtex - Download

@article{1e9f95c43f144dd9b4b25d291881d96d,
title = "The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII",
abstract = "Hydrophobins are surface-active proteins produced by filamentous fungi. They have amphiphilic structures and form multimers in aqueous solution to shield their hydrophobic regions. The proteins rearrange at interfaces and self-assemble into films that can show a very high degree of structural order. Little is known on dynamics of multimer interactions in solution and how this is affected by other components. In this work we examine the multimer dynamics by stopped-flow fluorescence measurements and F{\"o}rster Resonance Energy Transfer (FRET) using the class II hydrophobin HFBII. The half-life of exchange in the multimer state was 0.9 s at 22 °C with an activation energy of 92 kJ/mol. The multimer exchange process of HFBII was shown to be significantly affected by the closely related HFBI hydrophobin, lowering both activation energy and half-life for exchange. Lower molecular weight surfactants interacted in very selective ways, but other surface active proteins did not influence the rates of exchange. The results indicate that the multimer formation is driven by specific molecular interactions that distinguish different hydrophobins from each other.",
keywords = "Fluorescence, FRET, F{\"o}rster Resonance Energy Transfer, HFBI, HFBII, Hydophobin, Stopped-flow, Surfactant",
author = "M.S. Grun{\'e}r and A. Paananen and Szilvay, {G{\'e}za R.} and Linder, {M. B.}",
note = "This work wassupported by the Academy of Finland through its Centres of Excel-lence Programme (2014–2019) and under Projects No. 259034 and264493.",
year = "2017",
month = "7",
day = "1",
doi = "10.1016/j.colsurfb.2017.03.057",
language = "English",
volume = "155",
pages = "111--117",
journal = "Colloids and surfaces, B: Biointerfaces",
issn = "0927-7765",
publisher = "Elsevier Science B.V.",

}

RIS - Download

TY - JOUR

T1 - The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII

AU - Grunér, M.S.

AU - Paananen, A.

AU - Szilvay, Géza R.

AU - Linder, M. B.

N1 - This work wassupported by the Academy of Finland through its Centres of Excel-lence Programme (2014–2019) and under Projects No. 259034 and264493.

PY - 2017/7/1

Y1 - 2017/7/1

N2 - Hydrophobins are surface-active proteins produced by filamentous fungi. They have amphiphilic structures and form multimers in aqueous solution to shield their hydrophobic regions. The proteins rearrange at interfaces and self-assemble into films that can show a very high degree of structural order. Little is known on dynamics of multimer interactions in solution and how this is affected by other components. In this work we examine the multimer dynamics by stopped-flow fluorescence measurements and Förster Resonance Energy Transfer (FRET) using the class II hydrophobin HFBII. The half-life of exchange in the multimer state was 0.9 s at 22 °C with an activation energy of 92 kJ/mol. The multimer exchange process of HFBII was shown to be significantly affected by the closely related HFBI hydrophobin, lowering both activation energy and half-life for exchange. Lower molecular weight surfactants interacted in very selective ways, but other surface active proteins did not influence the rates of exchange. The results indicate that the multimer formation is driven by specific molecular interactions that distinguish different hydrophobins from each other.

AB - Hydrophobins are surface-active proteins produced by filamentous fungi. They have amphiphilic structures and form multimers in aqueous solution to shield their hydrophobic regions. The proteins rearrange at interfaces and self-assemble into films that can show a very high degree of structural order. Little is known on dynamics of multimer interactions in solution and how this is affected by other components. In this work we examine the multimer dynamics by stopped-flow fluorescence measurements and Förster Resonance Energy Transfer (FRET) using the class II hydrophobin HFBII. The half-life of exchange in the multimer state was 0.9 s at 22 °C with an activation energy of 92 kJ/mol. The multimer exchange process of HFBII was shown to be significantly affected by the closely related HFBI hydrophobin, lowering both activation energy and half-life for exchange. Lower molecular weight surfactants interacted in very selective ways, but other surface active proteins did not influence the rates of exchange. The results indicate that the multimer formation is driven by specific molecular interactions that distinguish different hydrophobins from each other.

KW - Fluorescence

KW - FRET

KW - Förster Resonance Energy Transfer

KW - HFBI

KW - HFBII

KW - Hydophobin

KW - Stopped-flow

KW - Surfactant

UR - http://www.scopus.com/inward/record.url?scp=85017434474&partnerID=8YFLogxK

U2 - 10.1016/j.colsurfb.2017.03.057

DO - 10.1016/j.colsurfb.2017.03.057

M3 - Article

VL - 155

SP - 111

EP - 117

JO - Colloids and surfaces, B: Biointerfaces

JF - Colloids and surfaces, B: Biointerfaces

SN - 0927-7765

ER -

ID: 12921796