Biophysical and molecular docking insight into interaction mechanism and thermal stability of human serum albumin isoforms with a semi-synthetic water-soluble camptothecin analog irinotecan hydrochloride

摘要: In the present work, we have examined binding parameters, thermodynamics, and stability of human serum albumin (HSA) isoforms at pH 7.4 9.0, using spectroscopic, calorimetric, molecular docking methods in presence water-soluble camptothecin analog irinotecan hydrochloride (CPT-11). We observed that CPT-11 binds to HSA through a static quenching procedure ground-state complex formation with N-isoform B-isoform. Hydrogen bond hydrophobic interactions are major governing forces participating protein-drug complex. To determine site within molecules, also performed experiments. explored CPT-11-mediated modulation by performing dynamic light scattering (DLS) differential scanning calorimetry (DSC) DLS DSC techniques used size melting point (Tm) HSA, which was decreased CPT-11. Therefore, plays an important role protein-ligand interactions. The study provides valuable information field pharmacokinetics, pharmaco-dynamics, drug discovery.