EFFICIENT AND SENSITIVE ANALYSIS OF BIOMOLECULAR INTERACTIONS BETWEEN PALBOCICLIB AND HUMAN SERUM ALBUMIN USING FLUORESCENCE QUENCHING MECHANISM

Objective: In this research, the interaction between Palbociclib (PC) and Human Serum Albumin (HSA) was examined using fluorescence spectroscopy, and the quenching mechanism was elucidated. Material and Method: HSA and PC stock solutions were prepared using 0.1 M pH 7.4 phosphate buffer solution and DMSO, respectively. In the protein-drug interaction experiment, the HSA concentration was fixed at 20 µM, and drug concentrations for the PC-HSA system were used between 0 and 40 µM. Result and Discussion: The interaction between PC and HSA was investigated at various temperatures using spectroscopic techniques. To comprehend the interaction process, experiments were carried out at different physiological pH levels and temperatures. Other parameters, including the number of binding sites, binding constants, and quenching constants, were calculated using the proper formulas. The van't Hoff equation was used to determine thermodynamic parameters such as entropy, Gibbs, and enthalpy at different temperatures.