期刊
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
卷 98, 期 1, 页码 12-19出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2009.10.002
关键词
Steady state and time resolved fluorescence; Excited-state intramolecular proton transfer; Robinetin; Egg yolk phosphatidylcholine liposome; Lipid peroxidation; Hemoglobin glycosylation
Recent years have witnessed burgeoning interest in plant flavonoids as novel therapeutic drugs targeting cellular membranes and proteins Motivated by this scenario, we explored the binding of robinetin (3,7,3',4',5'-pentahydroxyflavone, a bioflavonoid with remarkable 'two color' intrinsic fluorescence properties), with egg yolk phosphatidylcholine (EYPC) liposomes and normal human hemoglobin (HbA), using steady state and time resolved fluorescence spectroscopy Distinctive fluorescence signatures obtained for robinetin indicate its partitioning (K-p = 8.65 x 10(4)) into the hydrophobic core of the membrane lipid bilayer HbA-robinetin interaction was examined using both robinetin fluorescence and flavonoid-induced quenching of the protein tryptophan fluorescence Specific interaction with HbA was confirmed from three lines of evidence: (a) bimolecular quenching constant K-q >> diffusion controlled limit, (b) closely matched values of Stern-Volmer quenching constant and binding constant, (c) tau(0)/tau = 1 (where tau(0) and tau are the unquenched and quenched tryptophan fluorescence lifetimes, respectively) Absorption spectrophotometric assays reveal that robinetin inhibits EYPC membrane lipid peroxidation and HbA glycosylation with high efficiency. (C) 2009 Elsevier B.V. All rights reserved
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据