Study on Interaction of Coomassie Brilliant Blue G-250 with Bovine Serum Albumin by Multispectroscopic

Aim of present study was to investigate the interaction of coomassie brilliant blue G-250 (CBBG-250) with bovine serum albumin (BSA) by the multispectroscopic methods. Fluorescence-data showed that the complex of BSA-CBBG-250 forming made the intrinsic fluorescence quenching of BSA by CBBG-250 interaction. BSA also could interact with CBBG-250 and the CBBG-BSA complexes formed in a molar ratio of 1:1. UV-Vis results displayed that the apparent binding (association) constantK(a)of CBBG-250 with BSA was 5.03 x 10(4)(298 K), 3.04 x 10(4)(303 K), 2.84 x 10(4)(308 K) and 1.99 x 10(4)(313 K) L mol(-1)at different temperatures, respectively. The enthalpy change (oH) and entropy change (oS) were respectively calculated to be - 45.32 kJ mol(-1)and - 139.18 J mol(-1)K(-1), indicating that the hydrogen bonds andVan der Waalsforces played dominant roles in the interaction. The results showed that the diphenylamine structure and amino acid residues in the Coomassie Brilliant Blue G-250 had a strong Van der Waals force. The phenyl sulphonic acid group undergoes electrostatic interactions and hydrogen bond interactions with basic amino acids; the compound Coomassie Brilliant Blue G-250 can form a stable complex with BSA.

Automated summary

The study investigated the interaction of CBBG-250 with BSA through multispectroscopic methods. It was found that the two can form a stable complex through hydrogen bonds and Van der Waals forces. The diphenylamine structure in CBBG-250 and the amino acid residues play a significant role in the interaction.