dc.contributor.author |
Zare, Davoud |
|
dc.contributor.author |
McGrath, Kathryn M |
|
dc.contributor.author |
Allison, Jane R |
|
dc.coverage.spatial |
United States |
|
dc.date.accessioned |
2022-05-25T04:15:01Z |
|
dc.date.available |
2022-05-25T04:15:01Z |
|
dc.date.issued |
2015-06 |
|
dc.identifier.citation |
(2015). Biomacromolecules, 16(6), 1855-1861. |
|
dc.identifier.issn |
1525-7797 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59496 |
|
dc.description.abstract |
Protein adsorption at liquid-liquid interfaces is of immense relevance to many biological processes and dairy-based functional foods. Due to experimental limitations, however, there is still a remarkable lack of understanding of the adsorption mechanism, particularly at a molecular level. In this study, atomistic molecular dynamics simulations were used to elucidate the approach and adsorption mechanism of β-lactoglobulin (β-LG) at a decane-water interface. Through multiple independent simulations starting from three representative initial orientations of β-LG relative to the decane surface the rate at which β-LG approaches the oil/water interface is found to be independent of its initial orientation, and largely stochastic in nature. While the residues that first make contact with the decane and the final orientation of β-LG upon adsorption are similar in all cases, the adsorption process is driven predominantly by structural rearrangements that preserve the secondary structure but expose hydrophobic residues to the decane surface. This detailed characterization of the adsorption of β-LG at an oil/water interface should inform the design and development of novel encapsulation and delivery systems in the food and pharmaceutical sciences. |
|
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 |
Water |
|
dc.subject |
Alkanes |
|
dc.subject |
Oils |
|
dc.subject |
Lactoglobulins |
|
dc.subject |
Amino Acid Sequence |
|
dc.subject |
Molecular Sequence Data |
|
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 |
0306 Physical Chemistry (incl. Structural) |
|
dc.subject |
03 Chemical Sciences |
|
dc.subject |
06 Biological Sciences |
|
dc.subject |
09 Engineering |
|
dc.title |
Deciphering β-Lactoglobulin Interactions at an Oil-Water Interface: A Molecular Dynamics Study. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1021/acs.biomac.5b00467 |
|
pubs.issue |
6 |
|
pubs.begin-page |
1855 |
|
pubs.volume |
16 |
|
dc.date.updated |
2022-04-28T03:11:25Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
25989152 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/25989152 |
|
pubs.end-page |
1861 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
|
pubs.subtype |
Journal Article |
|
pubs.elements-id |
739555 |
|
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 |
2015-05-26 |
|