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Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications

Liang, Li, Tajmir-Riahi, H. A., Subirade, Muriel·2008·Biomacromolecules

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
Published
2007-12-08
Volume
9
Issue
1
Pages
50-56
ISSN
  • 1525-7797 (ISSN-L)
  • 1526-4602
OpenAlex
W1995931234
Cited by
472
References
1
FWCI
3.11
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications. https://app.cochat.ai/papers/10.1021/bm700728k
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Liang, L., Tajmir-Riahi, H. A., & Subirade, M. (2008). Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications. Biomacromolecules. https://doi.org/10.1021/bm700728k

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