Abstract
In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (
5d
) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug
5d
was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the
5d
and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and
5d
interaction was
s
tatic quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and
5d
interaction. The Förster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-
5d
interaction. This binding interaction study provided a basis to comprehend the binding interaction between
5d
and BSA. These results provided information about sites of BSA involved in its interaction with
5d
.