Spectroscopic study on the inherent binding information of cationic perfluorinated surfactant with bovine serum albumin

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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► FC-134 binds to tryptophan residue Trp-214 of BSA within site I (sub-domain IIA).
► FC-134 can quench BSA via a dynamic quenching mechanism with complex formation.
► The interaction with bovine serum albumin is found to be very strong.
► The study is expected to open us new applications of fluoro-surfactant.