Fluorescence study of BSA interaction with (R)-5-(3-(4-(azepan-1-ylmethyl)-1H-1,2,3-triazol-1-yl)prop-1-en-2-yl)-2-methylcyclohex-2-enone Chemistry

Abstract

Interaction between bovine serum albumin (BSA) and (R)-5-(3-(4-(azepan-1- -ylmethyl)-1H-1,2,3-triazol-1-yl)prop-1-en-2-yl)-2-methylcyclohex-2-enone(Triazole-A) was studied at 298 K and 308 K using fluorescence spectroscopy method. It was shown that the quenching mechanism of BSA by Triazole-A was initiated by a dynamic collision. Synchronous fluorescence measurements indicate that binding between Triazole-A and the protein does not lead to a change in the polarity of the microenvironment of the tryptophan and tyrosine residues.