Molecular Dynamics Simulation of β-Lactoglobulin at Different Oil/Water Interfaces.

Zare, D; Allison, JR; McGrath, KM

Molecular Dynamics Simulation of β-Lactoglobulin at Different Oil/Water Interfaces.

Zare, D Allison, JR McGrath, KM

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Publisher:: AMER CHEMICAL SOC
Publication Type:: Journal Article
Citation:: Biomacromolecules, 2016, 17, (5), pp. 1572-1581
Issue Date:: 2016-05-09

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Field	Value	Language
dc.contributor.author	Zare, D
dc.contributor.author	Allison, JR
dc.contributor.author	McGrath, KM
dc.date.accessioned	2022-07-29T05:23:30Z
dc.date.available	2022-07-29T05:23:30Z
dc.date.issued	2016-05-09
dc.identifier.citation	Biomacromolecules, 2016, 17, (5), pp. 1572-1581
dc.identifier.issn	1525-7797
dc.identifier.issn	1526-4602
dc.identifier.uri	http://hdl.handle.net/10453/159356
dc.description.abstract	Controlling and manipulating protein behavior at an interface is of immense relevance to a broad range of physicochemical and biological phenomena and technological processes. Although many experimental studies have contributed to rapid progress in the fundamental knowledge of protein behavior at interfaces, detailed molecular-level understanding of the mechanism of protein adsorption at an interface is still remarkably lacking. In this study, atomistic molecular dynamics simulations were used to characterize the adsorption of β-lactoglobulin at two different oil/water (O/W) interfaces, where the oil was either the marginally hydrophilic octanol or the more hydrophilic triolein, and the results were compared to those of a previous study utilizing the hydrophobic oil decane. Both the approach to the surface and the mechanism of adsorption depend upon the hydrophilicity of the oil and the interfacial tension of the O/W interface, with the nature of the adsorption, the accompanying structural changes, and the energetic driving force differing markedly between the different oils. Intriguingly, the behavior of the protein resembles that predicted for a soft spherical particle at an O/W interface. The results are also in agreement with key experimental findings, particularly the observation that proteins undergo more conformational change upon adsorption to hydrophobic surfaces, flattening out to expose hydrophobic interior residues to the surface, and that a thicker layer of native-like adsorbed protein forms at hydrophilic surfaces, and reveal structural and mechanistic detail behind each mechanism of adsorption.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	AMER CHEMICAL SOC
dc.relation.ispartof	Biomacromolecules
dc.relation.isbasedon	10.1021/acs.biomac.5b01709
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	03 Chemical Sciences, 06 Biological Sciences, 09 Engineering
dc.subject.classification	Polymers
dc.subject.mesh	Humans
dc.subject.mesh	Hydrophobic and Hydrophilic Interactions
dc.subject.mesh	Lactoglobulins
dc.subject.mesh	Molecular Dynamics Simulation
dc.subject.mesh	Oils
dc.subject.mesh	Protein Conformation
dc.subject.mesh	Surface Properties
dc.subject.mesh	Surface Tension
dc.subject.mesh	Water
dc.subject.mesh	Humans
dc.subject.mesh	Water
dc.subject.mesh	Oils
dc.subject.mesh	Lactoglobulins
dc.subject.mesh	Protein Conformation
dc.subject.mesh	Surface Properties
dc.subject.mesh	Surface Tension
dc.subject.mesh	Molecular Dynamics Simulation
dc.subject.mesh	Hydrophobic and Hydrophilic Interactions
dc.title	Molecular Dynamics Simulation of β-Lactoglobulin at Different Oil/Water Interfaces.
dc.type	Journal Article
utslib.citation.volume	17
utslib.location.activity	United States
utslib.for	03 Chemical Sciences
utslib.for	06 Biological Sciences
utslib.for	09 Engineering
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/DVC (Research)
utslib.copyright.status	closed_access	*
dc.date.updated	2022-07-29T05:23:24Z
pubs.issue	5
pubs.publication-status	Published
pubs.volume	17
utslib.citation.issue	5

Abstract:

Controlling and manipulating protein behavior at an interface is of immense relevance to a broad range of physicochemical and biological phenomena and technological processes. Although many experimental studies have contributed to rapid progress in the fundamental knowledge of protein behavior at interfaces, detailed molecular-level understanding of the mechanism of protein adsorption at an interface is still remarkably lacking. In this study, atomistic molecular dynamics simulations were used to characterize the adsorption of β-lactoglobulin at two different oil/water (O/W) interfaces, where the oil was either the marginally hydrophilic octanol or the more hydrophilic triolein, and the results were compared to those of a previous study utilizing the hydrophobic oil decane. Both the approach to the surface and the mechanism of adsorption depend upon the hydrophilicity of the oil and the interfacial tension of the O/W interface, with the nature of the adsorption, the accompanying structural changes, and the energetic driving force differing markedly between the different oils. Intriguingly, the behavior of the protein resembles that predicted for a soft spherical particle at an O/W interface. The results are also in agreement with key experimental findings, particularly the observation that proteins undergo more conformational change upon adsorption to hydrophobic surfaces, flattening out to expose hydrophobic interior residues to the surface, and that a thicker layer of native-like adsorbed protein forms at hydrophilic surfaces, and reveal structural and mechanistic detail behind each mechanism of adsorption.

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http://hdl.handle.net/10453/159356