1. Deciphering β-Lactoglobulin Interactionsat an Oil–Water Interface: A Molecular Dynamics Study.
- Author
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Davoud Zare, Kathryn M. McGrath, and Jane R. Allison
- Subjects
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LACTOGLOBULINS , *OIL-water interfaces , *MOLECULAR dynamics , *ADSORPTION (Chemistry) , *FUNCTIONAL foods , *DRUG delivery systems , *DRUG development , *DRUG design - Abstract
Protein adsorption at liquid–liquidinterfaces is of immenserelevance to many biological processes and dairy-based functionalfoods. Due to experimental limitations, however, there is still aremarkable lack of understanding of the adsorption mechanism, particularlyat a molecular level. In this study, atomistic molecular dynamicssimulations were used to elucidate the approach and adsorption mechanismof β-lactoglobulin (β-LG) at a decane–water interface.Through multiple independent simulations starting from three representativeinitial orientations of β-LG relative to the decane surfacethe rate at which β-LG approaches the oil/water interface isfound to be independent of its initial orientation, and largely stochasticin nature. While the residues that first make contact with the decaneand the final orientation of β-LG upon adsorption are similarin all cases, the adsorption process is driven predominantly by structuralrearrangements that preserve the secondary structure but expose hydrophobicresidues to the decane surface. This detailed characterization ofthe adsorption of β-LG at an oil/water interface should informthe design and development of novel encapsulation and delivery systemsin the food and pharmaceutical sciences. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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