Spectroscopic investigation on the interaction of direct yellow-27 with protein (BSA)

Abstract

Direct yellow 27 (DY-27) interaction with bovine serum albumin (BSA) was investigated using multi-spectroscopic techniques to understand the toxicity mechanism. Fluorescence quenching of BSA by DY-27 was observed as a result of the formation of a BSA-DY27 complex with a binding constant of 1.19 × 105 M-1 and followed a static quenching mechanism with a quenching constant Ksv of 7.25 × 104 M-1. The far UV circular dichroism spectra revealed the conformational changes in the secondary structure of BSA in the presence of DY-27. The calculated average lifetime of BSA is 6.04 ns and is nearly constant (5.99 ns) in the presence of dye and supports the proposed quenching mechanism. The change in free energy (ΔG) was calculated to be -28.96 kJ mol-1 and confirmed the spontaneity of the binding process. Further, docking studies have been conducted to gain more insights into the interactions between DY-27 and serum albumin.