采用光谱法研究黄芩素-牛血清白蛋白复合物与 Cu2+或 Fe3+的相互作用。
Characterization of the baicalein-bovine serum albumin complex without or with Cu2+ or Fe3+ by spectroscopic approaches.
机构信息
College of Chemistry and Chemical Engineering, Luoyang Normal University, Longmen Road 71#, Luoyang 471022, China.
出版信息
Eur J Med Chem. 2011 Feb;46(2):588-99. doi: 10.1016/j.ejmech.2010.11.038. Epub 2010 Dec 1.
The binding of baicalein to bovine serum albumin (BSA) in the absence and presence of Cu2+ or Fe3+ in aqueous solution has been studied by fluorescence, synchronous fluorescence, ultraviolet-visible (UV-vis) spectra, circular dichroism (CD) and the three-dimensional (3D) fluorescence at pH 7.40. The decrease of the binding constant in the presence of Cu2+ or Fe3+ may result from the competition of the metal ions and baicalein binding to BSA. The effect of baicalein on the conformation of BSA was analyzed using UV, CD, fluorescence and three-dimensional (3D) fluorescence. These results indicate that the binding of baicalein to BSA causes apparent change in the secondary structure of BSA, but does not affect the polarity around the chromophore molecule.
在 pH 7.40 条件下，通过荧光、同步荧光、紫外可见（UV-vis）光谱、圆二色性（CD）和三维（3D）荧光研究了黄芩素在水溶液中与牛血清白蛋白（BSA）结合的情况，以及在存在 Cu2+或 Fe3+的情况下的结合情况。在存在 Cu2+或 Fe3+的情况下，结合常数的降低可能是由于金属离子与黄芩素与 BSA 结合的竞争所致。利用紫外、CD、荧光和三维（3D）荧光分析了黄芩素对 BSA 构象的影响。这些结果表明，黄芩素与 BSA 的结合导致 BSA 的二级结构发生明显变化，但不影响发色团分子周围的极性。
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