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Updated: Sep 10, 2025

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Synthesis of 7-hydroxy coumarin derivatives and interaction with bovine serum albumin by multi-spectroscopic studies
Furkan Meletli1, Bengü Sema Mutafoğlu1, Mücahit Özdemir1
1Department of Chemistry, Faculty of Science, Marmara University, Istanbul, Turkey.
Abstract:
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.
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