Insights on the in-vitro binding interaction between donepezil and bovine serum albumin

• Published in: BMC chemistry Vol. 17; no. 1; p. 31
• Main Authors: El Gammal, Reem N., Elmansi, Heba, El-Emam, Ali A., Belal, Fathalla, Elzahhar, Perihan A., Belal, Ahmed S. F., Hammouda, Mohammed E. A.
• Format: Journal Article
• Language: English
• Published: Cham Springer International Publishing 06.04.2023; BioMed Central Ltd; Springer Nature B.V; BMC
• Subjects: Albumin; Binding sites; Bovine serum albumin; Cattle; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Donepezil; Energy transfer; Enthalpy; Fluorescence; Fluorescence resonance energy transfer; Fluorimetry; Fourier transform infrared; Fourier transforms; Molecular docking; Parameters; Quenching; Serum albumin; Spectrophotometry; Synchronous fluorimetry; Toxicity; Bovine serum albumin; Synchronous fluorimetry; Fluorescence resonance energy transfer; Fourier transform infrared; Donepezil; Molecular docking
• ISSN: 2661-801X; 2661-801X
• DOI: 10.1186/s13065-023-00944-z

In this work, the binding mechanism between donepezil (DNP) and bovine serum albumin (BSA) was established using several techniques, including fluorimetry, UV- spectrophotometry, synchronous fluorimetry (SF), fourier transform infrared (FTIR), fluorescence resonance energy transfer (FRET) besides molecular docking study. The fluorescence quenching mechanism of DNP-BSA binding was a combined dynamic and static quenching. The thermodynamic parameters, binding forces, binding constant, and the number of binding sites were determined using a different range of temperature settings. Van't Hoff's equation was used to calculate the reaction parameters, including enthalpy change (ΔH ο ) and entropy change (ΔS ο ). The results pointed out that the DNP-BSA binding was endothermic. It was shown that the stability of the drug-protein system was predominantly due to the intermolecular hydrophobic forces. Additionally, the site probing method revealed that subdomain IIA (Site I) is where DNP and BSA's binding occurs. This was validated using a molecular docking study with the most stable DNP configuration. This study might help to understand DNP's pharmacokinetics profile and toxicity as well as provides crucial information for its safe use and avoiding its toxicity.