Self-Assembly and Conformational Changes of Hydrophobin Classes at the Air-Water Interface

Konrad Meister (Corresponding Author), Alexander Bäumer, Géza R. Szilvay, Arja Paananen, Huib J. Bakker

Research output: Contribution to journalArticleScientificpeer-review

13 Citations (Scopus)

Abstract

We use surface-specific vibrational sum-frequency generation spectroscopy (VSFG) to study the structure and self-assembling mechanism of the class I hydrophobin SC3 from Schizophyllum commune and the class II hydrophobin HFBI from Trichoderma reesei. We find that both hydrophobins readily accumulate at the water–air interface and form rigid, highly ordered protein films that give rise to prominent VSFG signals. We identify several resonances that are associated with β-sheet structures and assign them to the central β-barrel core present in both proteins. Differences between the hydrophobin classes are observed in their interfacial self-assembly. For HFBI, we observe no changes in conformation upon adsorption to the water surface. For SC3, we observe an increase in β-sheet-specific signals that supports a surface-driven self-assembly mechanism in which the central β-barrel remains intact and stacks into a larger-scale architecture, amyloid-like rodlets.
Original languageEnglish
Pages (from-to)4067-4071
JournalThe Journal of Physical Chemistry Letters
Volume7
Issue number20
DOIs
Publication statusPublished - 2016
MoE publication typeA1 Journal article-refereed

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Self assembly
self assembly
Vibrational spectra
Water
air
Air
Spectroscopy
water
proteins
Proteins
assembling
surface water
Amyloid
spectroscopy
Conformations
Adsorption
adsorption
1-(heptafluorobutyryl)imidazole

Cite this

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title = "Self-Assembly and Conformational Changes of Hydrophobin Classes at the Air-Water Interface",
abstract = "We use surface-specific vibrational sum-frequency generation spectroscopy (VSFG) to study the structure and self-assembling mechanism of the class I hydrophobin SC3 from Schizophyllum commune and the class II hydrophobin HFBI from Trichoderma reesei. We find that both hydrophobins readily accumulate at the water–air interface and form rigid, highly ordered protein films that give rise to prominent VSFG signals. We identify several resonances that are associated with β-sheet structures and assign them to the central β-barrel core present in both proteins. Differences between the hydrophobin classes are observed in their interfacial self-assembly. For HFBI, we observe no changes in conformation upon adsorption to the water surface. For SC3, we observe an increase in β-sheet-specific signals that supports a surface-driven self-assembly mechanism in which the central β-barrel remains intact and stacks into a larger-scale architecture, amyloid-like rodlets.",
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Self-Assembly and Conformational Changes of Hydrophobin Classes at the Air-Water Interface. / Meister, Konrad (Corresponding Author); Bäumer, Alexander; Szilvay, Géza R.; Paananen, Arja; Bakker, Huib J.

In: The Journal of Physical Chemistry Letters, Vol. 7, No. 20, 2016, p. 4067-4071.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Self-Assembly and Conformational Changes of Hydrophobin Classes at the Air-Water Interface

AU - Meister, Konrad

AU - Bäumer, Alexander

AU - Szilvay, Géza R.

AU - Paananen, Arja

AU - Bakker, Huib J.

PY - 2016

Y1 - 2016

N2 - We use surface-specific vibrational sum-frequency generation spectroscopy (VSFG) to study the structure and self-assembling mechanism of the class I hydrophobin SC3 from Schizophyllum commune and the class II hydrophobin HFBI from Trichoderma reesei. We find that both hydrophobins readily accumulate at the water–air interface and form rigid, highly ordered protein films that give rise to prominent VSFG signals. We identify several resonances that are associated with β-sheet structures and assign them to the central β-barrel core present in both proteins. Differences between the hydrophobin classes are observed in their interfacial self-assembly. For HFBI, we observe no changes in conformation upon adsorption to the water surface. For SC3, we observe an increase in β-sheet-specific signals that supports a surface-driven self-assembly mechanism in which the central β-barrel remains intact and stacks into a larger-scale architecture, amyloid-like rodlets.

AB - We use surface-specific vibrational sum-frequency generation spectroscopy (VSFG) to study the structure and self-assembling mechanism of the class I hydrophobin SC3 from Schizophyllum commune and the class II hydrophobin HFBI from Trichoderma reesei. We find that both hydrophobins readily accumulate at the water–air interface and form rigid, highly ordered protein films that give rise to prominent VSFG signals. We identify several resonances that are associated with β-sheet structures and assign them to the central β-barrel core present in both proteins. Differences between the hydrophobin classes are observed in their interfacial self-assembly. For HFBI, we observe no changes in conformation upon adsorption to the water surface. For SC3, we observe an increase in β-sheet-specific signals that supports a surface-driven self-assembly mechanism in which the central β-barrel remains intact and stacks into a larger-scale architecture, amyloid-like rodlets.

U2 - 10.1021/acs.jpclett.6b01917

DO - 10.1021/acs.jpclett.6b01917

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JF - The Journal of Physical Chemistry Letters

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