ABSTRACT
Three new rimantadine Schiff bases [RSBs] were prepared, and then the interaction of RSBs with bovine serum albumin [BSA] was investigated using fluorescence, synchronous fluorescence, UV-vis absorption spectroscopy under physiological conditions. The results showed that the three RSBs effectively quenched the intrinsic fluorescence of BSA via static quenching. Binding constant [K[a]], number of binding sites [n], and the binding distance [r] between three RSBs and BSA were calculated by Stern-Volmer equation and Förster's theory in this study. According to the results of displacement experiments of site probes, it was considered that the binding sites were located in hydrophobic cavities in sub-domains IIA of BSA. What is more, synchronous fluorescence studies indicated that the hydrophobicity around tryptophan residues was increased with the addition of rimantadine-o-vanillin [ROV] and rimantadine-4-methoxy-salicylaldehyde [RMS], while there was no apparent change with the addition of rimantadine-salicylaldehyde [RS]