光学学报, 2017, 37 (11): 1130002, 网络出版: 2018-09-07   

米格列奈钙与牛血清白蛋白相互作用的光谱研究 下载: 898次

Study on Interaction Between Mitiglinide Calcium and Bovine Serum Albumin by Spectroscopy
作者单位
1 河海大学理学院, 江苏 南京 211100
2 南京航空航天大学理学院, 江苏 南京 210016
摘要
采用荧光光谱法、紫外可见吸收光谱法以及同步荧光光谱法研究了米格列奈钙与牛血清白蛋白(BSA)之间的相互作用。实验结果表明,米格列奈钙对牛血清白蛋白的荧光有较为明显的猝灭作用,其猝灭机制为动态猝灭,遵循Stern-Volmer方程;根据F rster的非辐射能量转移理论,计算出米格列奈钙分子与牛血清白蛋白分子的结合距离为5.461 nm;用同步荧光光谱技术探究了米格列奈钙对BSA构象的影响,结果发现,当激发和发射波长差为60 nm时,荧光峰位发生了微小的蓝移,说明BSA色氨酸残基附近的外围微环境受到了米格列奈钙分子的影响,极性减弱, BSA的疏水性增强。
Abstract
The interaction between mitiglinide calcium and bovine serum albumin (BSA) is studied by fluorescence emission spectroscopy, UV-visible absorption spectroscopy and synchronous fluorescence spectroscopy. Experimental results show that mitiglinide calcium leads to the fluorescence quenching of BSA, and the quenching mechanism is a dynamic quenching procedure according to the Stern-Volmer equation. The binding distance between mitiglinide calcium and BSA is calculated to be about 5.461 nm based on F rster theory. The effect of mitiglinide calcium on the conformation of BSA is studied by synchronous fluorescence spectroscopy. The results show that a slight blue shift is observed when the difference between excitation wavelength and emission wavelength is 60 nm. The blue shift indicates that the peripheral microenvironment near tryptophan residue of BSA is affected by the mitiglinine calcium molecule, which makes the polarity of the microenvironment decrease and the hydrophobicity of BSA increase.

张啸天, 张林, 朱卫华, 俞波. 米格列奈钙与牛血清白蛋白相互作用的光谱研究[J]. 光学学报, 2017, 37(11): 1130002. Xiaotian Zhang, Lin Zhang, Weihua Zhu, Bo Yu. Study on Interaction Between Mitiglinide Calcium and Bovine Serum Albumin by Spectroscopy[J]. Acta Optica Sinica, 2017, 37(11): 1130002.

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