Spectroscopic study on the inherent binding information of cationic perfluorinated surfactant with bovine serum albumin |
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Authors: | Ying Xi Wang [Author Vitae] [Author Vitae] Li Jiao Sheng [Author Vitae]Author Vitae] Zu Shun Xu [Author Vitae] |
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Affiliation: | Ministry-of-Education Key Laboratory for the Synthesis and Application of Organic Functional Molecules, College of Chemistry and Chemical Engineering, Hubei University, Wuhan 430062, Hubei, PR China |
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Abstract: | UV-vis, FT-IR, fluorescence and synchronous fluorescence spectra are applied to discuss the inherent binding information of model protein bovine serum albumin (BSA) with perfluorinated surfactant trimethyl-1-propanaminium iodide (FC-134). According to the results analyzed from Stern-Volmer equation, FC-134 can quench the fluorescence intensity of BSA via a dynamic quenching mechanism with complex formation. The thermodynamic parameters are calculated, revealing that hydrophobic force is the main interaction driven force. The binding constants and number of binding sites are also obtained. With the aid of site markers—warfarin and ibuprofen, we first report that FC-134 primarily binds to tryptophan residue Trp-214 of BSA within site I (sub-domain IIA). |
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Keywords: | FC-134 BSA FI-IR Fluorescence quenching Warfarin and ibuprofen |
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