Observation of pH-Induced Protein Reorientation at the Water Surface

Konrad Meister; Steven J. Roeter; Arja Paananen; Sander Woutersen; Jan Versluis; Géza R. Szilvay; Huib J. Bakker

doi:10.1021/acs.jpclett.7b00394

Observation of pH-Induced Protein Reorientation at the Water Surface

Konrad Meister (Corresponding Author), Steven J. Roeter, Arja Paananen, Sander Woutersen, Jan Versluis, Géza R. Szilvay, Huib J. Bakker

Research output: Contribution to journal › Article › Scientific › peer-review

20 Citations (Scopus)

Abstract

Hydrophobins are surface-active proteins that form a hydrophobic, water-repelling film around aerial fungal structures. They have a compact, particle-like structure, in which hydrophilic and hydrophobic regions are spatially separated. This surface property renders them amphiphilic and is reminiscent of synthetic Janus particles. Here we report surface-specific chiral and nonchiral vibrational sum-frequency generation spectroscopy (VSFG) measurements of hydrophobins adsorbed to their natural place of action, the air-water interface. We observe that hydrophobin molecules undergo a reversible change in orientation (tilt) at the interface when the pH is varied. We explain this local orientation toggle from the modification of the interprotein interactions and the interaction of hydrophobin with the water solvent, following the pH-induced change of the charge state of particular amino acids.

Original language	English
Pages (from-to)	1772-1776
Journal	The Journal of Physical Chemistry Letters
Volume	8
Issue number	8
DOIs	https://doi.org/10.1021/acs.jpclett.7b00394
Publication status	Published - 20 Apr 2017
MoE publication type	A1 Journal article-refereed

Funding

This work is part of the research program of the Stichting voor Fundamenteel Onderzoek der Materie (FOM), which is financially supported by the Nederlandse organisatie voor Wetenschappelijk Onderzoek (NWO). K.M. gratefully acknowledges the European Commission for funding through the award of a Marie Curie fellowship. A.P. and G.R.S. acknowledges support by the Academy of Finland through its Centres of Excellence Programme (2014-2019). Riitta Suihkonen is thanked for technical assistance with hydrophobins. S.J.R. and S.W. acknowledge the European Research Council (ERC) for funding through Grant 210999 and The Netherlands Organization for Scientific Research (NWO) for financially supporting this research.

Keywords

hydophobin
HFBII
air-water interface
interfacial behavior
vibrational sum-frequency generation spectroscopy
VSFGS
Water
Protein Structure, Secondary
Air
Adsorption
Fungal Proteins/chemistry
Hydrophobic and Hydrophilic Interactions
Protein Conformation

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10.1021/acs.jpclett.7b00394Licence: CC BY-NC-ND

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title = "Observation of pH-Induced Protein Reorientation at the Water Surface",

abstract = "Hydrophobins are surface-active proteins that form a hydrophobic, water-repelling film around aerial fungal structures. They have a compact, particle-like structure, in which hydrophilic and hydrophobic regions are spatially separated. This surface property renders them amphiphilic and is reminiscent of synthetic Janus particles. Here we report surface-specific chiral and nonchiral vibrational sum-frequency generation spectroscopy (VSFG) measurements of hydrophobins adsorbed to their natural place of action, the air-water interface. We observe that hydrophobin molecules undergo a reversible change in orientation (tilt) at the interface when the pH is varied. We explain this local orientation toggle from the modification of the interprotein interactions and the interaction of hydrophobin with the water solvent, following the pH-induced change of the charge state of particular amino acids.",

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AU - Meister, Konrad

AU - Roeter, Steven J.

AU - Paananen, Arja

AU - Woutersen, Sander

AU - Versluis, Jan

AU - Szilvay, Géza R.

AU - Bakker, Huib J.

PY - 2017/4/20

Y1 - 2017/4/20

N2 - Hydrophobins are surface-active proteins that form a hydrophobic, water-repelling film around aerial fungal structures. They have a compact, particle-like structure, in which hydrophilic and hydrophobic regions are spatially separated. This surface property renders them amphiphilic and is reminiscent of synthetic Janus particles. Here we report surface-specific chiral and nonchiral vibrational sum-frequency generation spectroscopy (VSFG) measurements of hydrophobins adsorbed to their natural place of action, the air-water interface. We observe that hydrophobin molecules undergo a reversible change in orientation (tilt) at the interface when the pH is varied. We explain this local orientation toggle from the modification of the interprotein interactions and the interaction of hydrophobin with the water solvent, following the pH-induced change of the charge state of particular amino acids.

AB - Hydrophobins are surface-active proteins that form a hydrophobic, water-repelling film around aerial fungal structures. They have a compact, particle-like structure, in which hydrophilic and hydrophobic regions are spatially separated. This surface property renders them amphiphilic and is reminiscent of synthetic Janus particles. Here we report surface-specific chiral and nonchiral vibrational sum-frequency generation spectroscopy (VSFG) measurements of hydrophobins adsorbed to their natural place of action, the air-water interface. We observe that hydrophobin molecules undergo a reversible change in orientation (tilt) at the interface when the pH is varied. We explain this local orientation toggle from the modification of the interprotein interactions and the interaction of hydrophobin with the water solvent, following the pH-induced change of the charge state of particular amino acids.

KW - hydophobin

KW - HFBII

KW - air-water interface

KW - interfacial behavior

KW - vibrational sum-frequency generation spectroscopy

KW - VSFGS

KW - Water

KW - Protein Structure, Secondary

KW - Air

KW - Adsorption

KW - Fungal Proteins/chemistry

KW - Hydrophobic and Hydrophilic Interactions

KW - Protein Conformation

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JO - The Journal of Physical Chemistry Letters

JF - The Journal of Physical Chemistry Letters

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ER -

Observation of pH-Induced Protein Reorientation at the Water Surface

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