研究姜黄素衍生物与牛血清白蛋白的结合情况。
Investigating the binding of curcumin derivatives to bovine serum albumin.
作者信息
Sahoo Bijaya Ketan, Ghosh Kalyan Sundar, Dasgupta Swagata
机构信息
Department of Chemistry, Indian Institute of Technology, Kharagpur, India.
出版信息
Biophys Chem. 2008 Feb;132(2-3):81-8. doi: 10.1016/j.bpc.2007.10.007. Epub 2007 Oct 23.
The interaction of bovine serum albumin (BSA) with isoxazolcurcumin (IOC) and diacetylcurcumin (DAC) has been investigated. Binding constants obtained were found to be in the 10(5) M(-1) range. Minor conformational changes of BSA were observed from circular dichroism (CD) and Fourier transformed infrared (FT-IR) studies on binding. Based on Förster's theory of non-radiation energy transfer, the average binding distance, r between the donor (BSA) and acceptors IOC and DAC was found to be 3.79 and 4.27 nm respectively. Molecular docking of isoxazolcurcumin and diacetylcurcumin with bovine serum albumin indicated that they docked close to Trp 213, which is within the hydrophobic subdomain.
已对牛血清白蛋白（BSA）与异恶唑姜黄素（IOC）和二乙酰姜黄素（DAC）的相互作用进行了研究。所获得的结合常数在10⁵ M⁻¹范围内。通过对结合进行圆二色性（CD）和傅里叶变换红外（FT-IR）研究，观察到了BSA的微小构象变化。基于Förster的非辐射能量转移理论，发现供体（BSA）与受体IOC和DAC之间的平均结合距离r分别为3.79和4.27 nm。异恶唑姜黄素和二乙酰姜黄素与牛血清白蛋白的分子对接表明，它们对接在靠近Trp 213的位置，该位置位于疏水亚结构域内。
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