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

ABSTRACT: 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.

SUBMITTER: El Gammal RN 

PROVIDER: S-EPMC10077752 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature