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

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.