Study on the Conformational Change of the Interaction Between Bovine Serum Albumin and Troxerutin by Fourier Transform Infrared Spectroscopy

Abstract

The conformational change of the binding interaction of troxerutin with bovine serum albumin (BSA) was investigated by Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The results showed that the secondary structure changes of BSA were changed by the addition of troxerutin. Combining the curve-fitting results of amide I bands, the alterations of protein secondary structure after drug complexation were quantitatively determined. The a-helix structure has a decrease of » 13 %, from 59-46 % and the b-sheet increased » 5 %, from 28-33 % and the b-turn increased » 8 %, from 13-21 % at high drug concentration. It is very significance to study the conformational change of interaction between troxerutin and serum albumin for understanding of troxerutin's toxicity and its distribution in the organism.