Akademik Veri Yönetim Sistemi
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, cilt.345, 2026 (SCI-Expanded, Scopus)
The interaction of 7-hydroxy-3-phenylcoumarin derivatives (K1-K5), synthesized via Perkin reaction with bovine serum albumin (BSA) was investigated. The UV–Vis and fluorescence spectroscopic analyses of coumarin derivatives with BSA revealed static quenching mechanisms for all compounds, with Stern-Volmer constants (Ksv) up to 5.87 × 105 M−1 and binding constants (Kb) ranging from 1.0 × 103 M−1 (K3) to 2.88 × 109 M−1 (K1) across 298–313 K. Specifically, K4 exhibited the most favorable binding to BSA, characterized by minimum Gibbs free energy value (ΔG° = −41.29 kJ mol−1) and a moderate binding constant (Kb = 173.36 × 105 M−1), indicating spontaneous and thermodynamically efficient interactions at 298 K. K2 and K5 also displayed affinity to the BSA (ΔG° = −29.12 and − 27.47 kJ mol−1 at 298 K, respectively), suggesting their potential suitability for serum-albumin-based delivery systems. Molecular docking supported these findings, identifying Sudlow's Site II (IIIA) as the preferred binding pocket, with binding energies ranging from −7.68 to −8.65 kcal/mol. Overall, all compounds exhibited promising experimental and theoretical interaction profiles, indicating that BSA could be utilized as a potential drug carrier.