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

作者：Yuhe Wang, Junfeng Li, Xuanda Li, Bingmiao Gao, Jiao Chen, Yun Tao Song · 发表于：Scientific Reports · 年份：2025 · DOI：10.1038/s41598-025-92607-3 · 被引用次数：17 · 研究领域：Protein Interaction Studies and Fluorescence Analysis、Neonatal Health and Biochemistry、Antibiotics Pharmacokinetics and Efficacy

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 × 10 3 M − 1 (CPT) to 101.30 × 10 3 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 ·K − 1 ), while irinotecan exhibits stronger binding dominated by electrostatic forces (ΔH = − 86.77 kJ·mol − 1 ) with significant entropy loss (ΔS = − 0.161 kJ·mol − 1 ·K − 1 ). Molecular docking confirms preferential binding at Sudlow site I of BSA, with hydrophobic interactions and hydrogen bonding as the primary driving forces. These findings provide a comprehensive understanding of CPT-BSA interactions, offering valuable insights for the design of albumin-based drug delivery systems with optimized pharmacokinetic profiles.