SPR and molecular modelling study of dipyridamole with bovine serum albumin (BSA) interaction
JOURNAL OF MOLECULAR STRUCTURE, cilt.1344, 2025 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 1344
- Basım Tarihi: 2025
- Doi Numarası: 10.1016/j.molstruc.2025.142941
- Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Chemical Abstracts Core, Chimica, Compendex, INSPEC
- İstanbul Üniversitesi Adresli: Evet
Özet
Determining protein-drug interactions is a critical aspect of drug discovery, as it plays a key role in evaluating pharmacokinetic profiles, physicochemical properties, serum concentrations, and the physiological activity of drug candidates. Therefore, this study aimed to rigorously investigate the interaction of the hydrophobic drug dipyridamole with bovine serum albumin (BSA) using both surface plasmon resonance (SPR) and computational molecular docking methods. In order to investigate the interactions between dipyridamole and BSA, the BSA protein was covalently bound to the surface of a cysteamine-activated gold-coated SPR chip. The SPR has been used to determine the interaction, dissociation rate constant (kd), association rate constant (ka), and binding affinity (KD). The kinetic and affinity parameters were calculated by binding the dipyridamole molecules at different concentrations that were injected into the system with BSA immobilised on the surface of the SPR chip. Low KD values indicate a high degree of affinity between the drug and protein molecules. The equilibrium constant (KD) value at 25 degrees C (5.054 x 10-6 M) indicated that dipiridamole binds to BSA slightly above normal binding values. Molecular docking studies were conducted to predict the binding regions of dipyridamole on bovine serum albumin (BSA) and to validate the experimental interaction data. The docking results identified binding sites I and II as the most favorable locations for dipyridamole on BSA. Additionally, hydrogen bonding and It-cation interactions were found to play key roles in stabilizing the dipyridamole-BSA complex.