Interaction of β-Lactoglobulin with resveratrol and its biological implications

被引:417
作者
Liang, Li [1 ]
Tajmir-Riahi, H. A. [2 ]
Subirade, Muriel [1 ]
机构
[1] Univ Laval, Chair Rech Canada Proteines Biosyst & Aliments Fo, INAF STELA, Ste Foy, PQ G1K 7P4, Canada
[2] Univ Quebec Trois Rivieres, Dept Chim Biol, Trois Rivieres, PQ G9A 5H7, Canada
关键词
D O I
10.1021/bm700728k
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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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页码:50 / 56
页数:7
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