山柰酚与人血清白蛋白的相互作用：荧光和圆二色性研究。
Interaction of kaempferol with human serum albumin: a fluorescence and circular dichroism study.
机构信息
Department of Physical Chemistry, Faculty of Chemistry, University of Bucharest, Bd. Regina Elisabeta, No. 4-12, Bucharest, Romania.
出版信息
J Pharm Biomed Anal. 2010 Feb 5;51(3):768-73. doi: 10.1016/j.jpba.2009.09.037. Epub 2009 Oct 1.
The interaction of kaempferol (kaemp), a natural flavonoid to which antioxidative, anti-inflammatory and cardio-protective biological activities have been attributed, with human serum albumin (HSA), the main in vivo transporter of exogenous substances, was investigated by steady-state, synchronous fluorescence and circular dichroism spectroscopies. The binding constant, K, and number of binding sites, n, were computed using literature models that showed satisfactory agreement and revealed a strong interaction (K approximately 3.5x10(5)M(-1), n approximately 1). The binding process was investigated at temperatures in the range 298-313K, allowing for the evaluation of the thermodynamic parameters, which indicate the occurrence of hydrogen bonding interactions. The distance between kaemp and the tryptophan residue of HSA was estimated at 2.7nm using Förster's theory of nonradiative resonance energy transfer. Using circular dichroism we evidenced some degree of HSA defolding upon binding.
通过稳态、同步荧光和圆二色光谱研究了山奈酚（kaemp）与人体血清白蛋白（HSA）的相互作用，山奈酚是一种天然类黄酮，具有抗氧化、抗炎和心脏保护的生物活性，HSA 是外源性物质的主要体内转运蛋白。使用文献模型计算了结合常数 K 和结合位点数 n，结果表明结合非常强（K 约为 3.5x10(5)M(-1)，n 约为 1），并且与实验值吻合良好。在 298-313K 的温度范围内研究了结合过程，从而可以评估热力学参数，这些参数表明氢键相互作用的发生。使用福斯特非辐射共振能量转移理论估算了山奈酚与 HSA 色氨酸残基之间的距离为 2.7nm。通过圆二色性，我们证明了结合时 HSA 一定程度的去折叠。
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