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<p>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<sub>b</sub>) ranging from 4.23 × 10<sup>3</sup> M<sup>− 1</sup> (CPT) to 101.30 × 10<sup>3</sup> M<sup>− 1</sup> (irinotecan), demonstrating significant drug binding selectivity. Thermodynamic analysis reveals distinct interaction mechanisms: topotecan binding is driven by hydrogen bonding (ΔH = − 10.96&#xa0;kJ·mol<sup>− 1</sup>) and hydrophobic interactions (ΔS = 0.066&#xa0;kJ·mol<sup>− 1</sup>·K<sup>− 1</sup>), while irinotecan exhibits stronger binding dominated by electrostatic forces (ΔH = − 86.77&#xa0;kJ·mol<sup>− 1</sup>) with significant entropy loss (ΔS = − 0.161&#xa0;kJ·mol<sup>− 1</sup>·K<sup>− 1</sup>). 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.</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年3月7日

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  • Yuhe Wang,
  • Junfeng Li,
  • Xuanda Li,
  • Bingmiao Gao,
  • Jiao Chen,
  • Yun Song

摘要

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 (Kb) 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·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.