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

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dc.contributor.author Zare, Davoud
dc.contributor.author Allison, Jane R
dc.contributor.author McGrath, Kathryn M
dc.coverage.spatial United States
dc.date.accessioned 2022-05-25T03:25:59Z
dc.date.available 2022-05-25T03:25:59Z
dc.date.issued 2016-05
dc.identifier.citation (2016). Biomacromolecules, 17(5), 1572-1581.
dc.identifier.issn 1525-7797
dc.identifier.uri https://hdl.handle.net/2292/59495
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.medium Print-Electronic
dc.language eng
dc.publisher American Chemical Society (ACS)
dc.relation.ispartofseries Biomacromolecules
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher.
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm
dc.subject Humans
dc.subject Water
dc.subject Oils
dc.subject Lactoglobulins
dc.subject Protein Conformation
dc.subject Surface Properties
dc.subject Surface Tension
dc.subject Molecular Dynamics Simulation
dc.subject Hydrophobic and Hydrophilic Interactions
dc.subject Science & Technology
dc.subject Life Sciences & Biomedicine
dc.subject Physical Sciences
dc.subject Biochemistry & Molecular Biology
dc.subject Chemistry, Organic
dc.subject Polymer Science
dc.subject Chemistry
dc.subject OIL-WATER INTERFACE
dc.subject RADIATION CIRCULAR-DICHROISM
dc.subject PARTICLE MESH EWALD
dc.subject CONFORMATIONAL-CHANGES
dc.subject FLUID INTERFACES
dc.subject FORCE-FIELD
dc.subject EMULSION INTERFACES
dc.subject PROTEIN ADSORPTION
dc.subject SOFT PARTICLES
dc.subject HYDROPHOBIN
dc.subject 0306 Physical Chemistry (incl. Structural)
dc.subject 0601 Biochemistry and Cell Biology
dc.subject 03 Chemical Sciences
dc.subject 06 Biological Sciences
dc.subject 09 Engineering
dc.title Molecular Dynamics Simulation of β-Lactoglobulin at Different Oil/Water Interfaces.
dc.type Journal Article
dc.identifier.doi 10.1021/acs.biomac.5b01709
pubs.issue 5
pubs.begin-page 1572
pubs.volume 17
dc.date.updated 2022-04-28T03:00:30Z
dc.rights.holder Copyright: The author en
dc.identifier.pmid 27075297 (pubmed)
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/27075297
pubs.end-page 1581
pubs.publication-status Published
dc.rights.accessrights http://purl.org/eprint/accessRights/RetrictedAccess en
pubs.subtype Research Support, Non-U.S. Gov't
pubs.subtype Journal Article
pubs.elements-id 739553
pubs.org-id Science
pubs.org-id Biological Sciences
dc.identifier.eissn 1526-4602
pubs.record-created-at-source-date 2022-04-28
pubs.online-publication-date 2016-04-25


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