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叶菌唑与HSA和BSA相互作用的荧光光谱分析
发表时间：2013-12-31 浏览量：2261 下载量：845
| 全部作者： | 汪海飞，张文静，潘柳萌，张丰，刘维屏 |
| 作者单位： | 浙江大学环境与资源学院 |
| 摘 要： | 为评估叶菌唑暴露对人及哺乳动物的危害，通过稳态荧光及时间分辨荧光光谱技术，比较分析叶菌唑与人血清蛋白（human serum albumin, HSA）和牛血清蛋白（bovine serum albumin, BSA）的相互作用。叶菌唑能够导致HSA和BSA内源性荧光显著猝灭，其猝灭方式为静态猝灭。叶菌唑的结合会引起HSA和BSA的荧光光谱红移，这说明了HSA和BSA蛋白内部微环境的显著变化，显示了叶菌唑对HSA及BSA蛋白构象的毒性作用。叶菌唑主要通过氢键和范德华力与HSA及BSA相互作用，叶菌唑与HSA的结合能力大于其与BSA的结合能力。 |
| 关 键 词： | 环境化学；叶菌唑；人血清蛋白；牛血清蛋白；相互作用；荧光光谱分析 |
| Title： | Study on the interactions of metconazole with HSA and BSA by spectrofluorimetry |
| Author： | WANG Haifei, ZHANG Wenjing, PAN Liumeng, ZHANG Feng, LIU Weiping |
| Organization： | College of Environmental and Resource Sciences, Zhejiang University |
| Abstract： | To evaluate the risks of the exposure of metconazole to the health of human and mammals, the interactions of metconazole with human serum albumin (HSA) and bovine serum albumin (BSA) were comparatively investigated by the combination of steady-state fluorescence and time-resolved fluorescence techniques. Metconazole could significantly quench the intrinsic fluorescence of HSA and BSA via the static quenching mode. With the binding of metconazole, the fluorescence spectra of HSA and BSA appeared red shifts, indicating the micro-environment of the HSA and BSA proteins changed, which manifested toxic effect on the conformation of HSA and BAS. Their interactions were mainly contributed by the van der Waals forces and hydrogen bonding, while metconazole had a stronger binding interaction with HSA than with BSA. |
| Key words： | environmental chemistry; metconazole; human serum albumin; bovine serum albumin; interaction; spectrofluorimetry |
| 发表期数： | 2013年12月第24期 |
| 引用格式： | 汪海飞，张文静，潘柳萌，等. 叶菌唑与HSA和BSA相互作用的荧光光谱分析[J]. 中国科技论文在线精品论文，2013，6（24）：2339-2345. |
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