费斯特共振能量转移
牛血清白蛋白
化学
荧光
色氨酸
荧光团
猝灭(荧光)
血清白蛋白
光化学
色谱法
生物化学
氨基酸
量子力学
物理
作者
Zongqing Bai,Yushuang Liu,Ping Zhang,Jun Guo,Yuxing Ma,Xiaoling Yun,Xiujian Zhao,Ruibo Zhong,Feng Zhang
出处
期刊:Luminescence
[Wiley]
日期:2015-08-19
卷期号:31 (3): 688-693
被引量:25
摘要
Physical binding-mediated organic dye direct-labelling of proteins could be a promising technology for bio-nanomedical applications. Upon binding, it was found that fluorescence resonance energy transfer (FRET) occurred between donor bovine serum albumin (BSA; an amphiphilic protein) and acceptor fluoresceinamine (FA; a hydrophobic fluorophore), which could explain fluorescence quenching found for BSA. FRET efficiency and the distance between FA and BSA tryptophan residues were determined to 17% and 2.29 nm, respectively. Using a spectroscopic superimposition method, the saturated number of FAs that bound to BSA was determined as eight to give a complex formula of FA8-BSA. Finally, molecular docking between BSA and FA was conducted, and conformational change that occurred in BSA upon binding to FA molecules was also studied by three-dimensional fluorescence microscopy.
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