引用本文:
马萍, 迟燕华, 庄稼, 邓建军, 周磊. 人血清白蛋白与酸性铬兰K相互作用机理的光谱学[J]. 应用化学,
2008, 25(9): 1032-1036.
Citation: MA Ping, CHI Yan-Hua, ZHUANG Jia, DENG Jian-Jun, ZHOU Lei. Spectroscopic Study on Interactions Between Human Serum Albumin and Acidic Chromic Blue K[J]. Chinese Journal of Applied Chemistry, 2008, 25(9): 1032-1036.
Citation: MA Ping, CHI Yan-Hua, ZHUANG Jia, DENG Jian-Jun, ZHOU Lei. Spectroscopic Study on Interactions Between Human Serum Albumin and Acidic Chromic Blue K[J]. Chinese Journal of Applied Chemistry, 2008, 25(9): 1032-1036.
人血清白蛋白与酸性铬兰K相互作用机理的光谱学
摘要:
采用荧光光谱法、紫外可见吸收光谱和傅立叶变换红外光谱法(FT-IR)研究了模拟生理条件下人血清白蛋白(HSA)与酸性铬兰K(ACBK)的相互作用。根据荧光猝灭数据,HSA与ACBK有一个结合位点,结合常数为2.3×104 L/mol;根据Förster能量转移理论,求得ACBK与HSA上氨基酸残基间的距离r=3.46 nm;运用蛋白质红外光谱酰胺Ⅰ带和酰胺Ⅲ带结合的方法定量测定了HSA与ACBK作用后二级结构的变化。结果发现,HSA与ACBK的结合使蛋白质分子中的肽链部分展开,α螺旋结构明显减少约9%,β-折叠减少约2%,而β-转角和无规卷曲分别增加了约6%和5%。结果说明,说明二级结构由α螺旋和β-折叠向β-转角和无规卷曲结构转变,分子结构的松散程度增加;根据荧光光谱和红外光谱的分析结果探讨了HSA与ACBK结合,结果表明,ACBK分子中苯环的疏水性使其与HSA疏水腔中的氨基酸残基发生相互作用。
English
Spectroscopic Study on Interactions Between Human Serum Albumin and Acidic Chromic Blue K
Abstract:
The interactions between human serum albumin(HSA) and acidic chromic blue K(ACBK) was investigated by fluorescence spectroscopy and Fourier transform infrared spectroscopy(FT-IR) under simulative physiological conditions.The quenching constants of HSA by ACBK suggested ACBK could quench the intrinsic fluorescence of HSA by static quenching.According to fluorescence resonance energy transfer(FRET),the distance and energy transfer efficiency(E) between the donor(HSA) and the acceptor(ACBK) were calculated to be 2.29 nm and 0.078,respectively.The relationship of fluorescence quenching and the changes of HSA secondary structure induced by ACBK binding was investigated by combining the results of fluorescence and FT-IR.The fluorescence results and FT-IR study suggested that hydrophobic interactions were the predominant intermolecular force and caused the secondary structure of HSA to change from α-helix and β-sheets to β-turns and random coils respectively.Upon HSA-ACBK complexing,the α-helix structure reduced by more than 9%,and the β-sheet reduced by 2%,while the β-turn increased by 6%,and the random coil increased by 5%.
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