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Fluorescence resonance energy transfer between bovine serum albumin and fluoresceinamine
Author(s) -
Bai Zhijun,
Liu Yushuang,
Zhang Ping,
Guo Jun,
Ma Yuxing,
Yun Xiaoling,
Zhao Xinmin,
Zhong Ruibo,
Zhang Feng
Publication year - 2016
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3012
Subject(s) - förster resonance energy transfer , bovine serum albumin , chemistry , fluorescence , tryptophan , fluorophore , quenching (fluorescence) , serum albumin , photochemistry , chromatography , biochemistry , amino acid , physics , quantum mechanics
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 FA 8 –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. Copyright © 2015 John Wiley & Sons, Ltd.