Dual quenching nature of bovine serum albumin and dopamine complex revealed using multi-spectral and docking studies.

[Display omitted] In the present study, dopamine interaction with bovine serum albumin was investigated using fluorescence, UV–vis, Raman, CV, FTIR and molecular modeling techniques. The fluorescence study of the quenching was carried out at an excitation wavelength of 296.0 nm, and the emission was measured in the range of 300–600 nm. BSA was quenched through both static and dynamic mechanisms. Thermodynamic parameters were derived to study the binding forces involved. The average binding distance between BSA and dopamine was determined using FÖrsters theory. Lifetime measurements, synchronous fluorescence and 3D spectra supported the hypotheses derived from the fluorescence data. The presence of some common co-existent drugs and the effect of essential biological metal ions were also investigated. [ABSTRACT FROM AUTHOR]