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This work presents the studies of the interactions of two newly synthesized anticancer drug candidates (AR2 and AR3, analogues of WZ4002) with anilinopyrimidine scaffolding core moiety with bovine serum albumin (BSA) and human serum albumin (HSA) using UV-Vis absorption, fluorescence spectroscopy and molecular docking techniques. UV-Vis spectroscopy reveals an interaction of the two compounds with the albumins. Synchronous and regular fluorescence spectra of these two compounds show an exhibition of a static quenching process as formation of both BSA/HSA-drug complexes. The calculated binding constants with the correction of the absorptions of these compounds at 280 nm were moderately large. The calculated thermodynamic parameters (ΔH, ΔS and ΔG) reveal interaction forces between these two compounds and BSA/HSA fluorescence sites (reside in site I sub-domain IIA) are through Van der Waals (hydrophobic) and hydrogen binding forces which was also observed in the molecular docking study.

UV-Vis, Fluorescence and Molecular Docking Studies on the Binding of Bovine and Human Serum Albumins with Novel Anticancer Drug Candidates