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Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications
Abstract
Beta-lactoglobulin (beta-LG), the major whey protein in the milk of ruminants, has a high affinity for a wide range of compounds. Resveratrol (3,5,4'-trihydroxystilbene), a natural polyphenolic compound found in grapes and red wine, exhibits many physiological effects associated with health benefits. In this study, the interaction of resveratrol with beta-LG was investigated using circular dichroism, fluorescence and UV-vis absorbance. Self-association of resveratrol possibly occurs at high concentrations. Resveratrol interacts with beta-LG to form 1:1 complexes. Resveratrol is bound to the surface of the protein because beta-LG-bound polyphenol is in a weaker hydrophobic environment relative to 75% ethanol. The binding constant for the resveratrol-beta-LG interaction is between 10(4) and 10(6) M (-1), as determined by protein or polyphenol fluorescence. The beta-LG-resveratrol interaction may compete with self-association of both the polyphenol and the protein. It has no apparent influence on beta-LG secondary structure but partially disrupts tertiary structure. Complexing with beta-LG provides a slight increase in the photostability of resveratrol and a significant increase in its hydrosolubility.
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Metadata
- Authors
- Liang, L., Tajmir-Riahi, H. A., & Subirade, M.
- Venue
- Biomacromolecules
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-12-08
- Volume
- 9
- Issue
- 1
- Pages
- 50-56
- ISSN
- 1525-7797 (ISSN-L)
- 1526-4602
- OpenAlex
- W1995931234
- Cited by
- 472
- References
- 40
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- closed
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