摘要
该文在模拟生理条件下,采用荧光光谱法、三维荧光光谱法以及圆二色谱法,研究氨基比林(PYM)与牛血清白蛋白(BSA)之间的相互作用。研究结果表明PYM对BSA有强烈的荧光猝灭作用,其荧光猝灭机制为静态猝灭。由热力学参数判定PYM和BSA的主要作用力为氢键和范德华力,并且相互作用是自发进行的。根据F觟rster的偶极-偶极非辐射能量转移理论可以得出PYM与BSA之间的结合距离为2.09 nm。利用三维荧光光谱和圆二色谱技术,分析PYM对BSA蛋白构象的影响,表明PYM与BSA相互作用后使BSA的微环境和构象发生改变。
The interaction between aminopyrine （PYM） and bovine serum albumin （BSA） were investigated with fluorescence spectroscopy,three -dimensional fluorescence spectroscopy,circular dichroism （CD） spectrum and under imitated physiological conditions. The results show that PYM could strongly quenching the fluorescence of BSA and the quenching process is a static process. The thermoclynamic parameters demonstrated that PYM can spontaneously bind with BSA through hydrogen bonds and Van der Waals forces. The binding distance of 2.09 nm between PYM and BSA was obtained by the Forster’ s theory on resonance energy transfer. Three -dimensional fluorescence spectroscopy and circular dichroism （CD） spectrum show that PYM could change the miro-enviroment and conformation of BSA.
出处
《中国测试》
北大核心
2017年第9期74-80,共7页
China Measurement & Test
基金
国家自然科学基金(21463016)
内蒙古自然科学基金(2013MS0209)
内蒙古高等学校科学研究项目(NJZZ14160)
关键词
氨基比林
牛血清白蛋白
荧光猝灭
三维荧光光谱
圆二色谱
aminopyrine
bovine serum albumin
fluorescence quenching
three-dimensional fluo-rescence spectroscopy
circular dichroism spectrum
