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  • Title: Fluorescence resonance energy transfer between bovine serum albumin and fluoresceinamine.
    Author: Bai Z, Liu Y, Zhang P, Guo J, Ma Y, Yun X, Zhao X, Zhong R, Zhang F.
    Journal: Luminescence; 2016 May; 31(3):688-93. PubMed ID: 27037968.
    Abstract:
    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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