Spectroscopic and molecular docking studies on binding interactions of camptothecin drugs with bovine serum albumin.

ABSTRACT: This study investigates the binding interactions between bovine serum albumin (BSA) and camptothecin (CPT) drugs (camptothecin, 10-hydroxycamptothecin, topotecan, and irinotecan) using UV-Vis spectroscopy, fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, and molecular docking techniques. The fluorescence quenching of BSA by CPT drugs follows a static mechanism, with binding constants (K_b) ranging from 4.23 × 10³ M^- 1 (CPT) to 101.30 × 10³ M^- 1 (irinotecan), demonstrating significant drug binding selectivity. Thermodynamic analysis reveals distinct interaction mechanisms: topotecan binding is driven by hydrogen bonding (ΔH = - 10.96 kJ·mol^- 1) and hydrophobic interactions (ΔS = 0.066 kJ·mol^- 1

SUBMITTER: Wang Y 

PROVIDER: S-EPMC11889159 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature