分子光谱法研究橙皮苷甲基醚与人血清白蛋白的相互作用。
Molecular spectroscopic on interaction between Methyl hesperidin and Buman serum albumin.
机构信息
School of Materials and Chemical Engineering, Xi'an Technological University, Xi'an 710032, China.
出版信息
Spectrochim Acta A Mol Biomol Spectrosc. 2013 Feb;102:200-4. doi: 10.1016/j.saa.2012.10.012. Epub 2012 Oct 23.
The interaction of Methyl hesperidin (MH) with Buman serum albumin was studied by spectroscopic methods including Fluorescence quenching technology, UV absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The result of fluorescence titration revealed that Methyl hesperidin could quench the intrinsic fluorescence of BSA and the quenching mechanism should be a combined quenching process. The binding constants at three temperatures (296, 303, and 310 K) were 1.82, 2.69, and 3.4 × 10(4)L mol(-1), respectively. The distance between donor (BSA) and acceptor (MH) was 5.54 nm according to the Förster theory of non-radiation energy transfer. In addition, FT-IR spectroscopy showed that the binding of MH to BSA changed the secondary structure of protein.
采用荧光猝灭技术、紫外吸收光谱和傅里叶变换红外（FT-IR）光谱法，在模拟生理条件下研究了甲基橙皮苷（MH）与牛血清白蛋白（BSA）的相互作用。荧光滴定结果表明，甲基橙皮苷可以猝灭 BSA 的内源荧光，猝灭机制应为复合猝灭过程。三个温度（296、303 和 310 K）下的结合常数分别为 1.82、2.69 和 3.4×10(4)L mol(-1)。根据福斯特非辐射能量转移理论，供体（BSA）和受体（MH）之间的距离为 5.54nm。此外，FT-IR 光谱表明，MH 与 BSA 的结合改变了蛋白质的二级结构。
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