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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-23 18:21 |
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Conference: Bucharest University Faculty of Physics 2022 Meeting
Section: Biophysics; Medical Physics
Title:
Effect of flavonoids on physico-chemical properties of aldehyde dehidrogenase
Authors:
Diana L. STAN, Raluca TÎRCĂ, Daria FLOREA, Georgiana CHIRA, Nicoleta CAZACU, Claudia G. CHILOM
*
Affiliation:
University of Bucharest, Faculty of Physics
E-mail
claudia-gabriela.chilom@unibuc.ro
Keywords:
protein-ligand interaction, driving forces, molecular docking, structure stabilization
Abstract:
Flavonoids are a class of molecules identified in many natural plants with promising biological activities such as antioxidant, anti-inflammatory, and anti-cancer effects. This study aims to investigate the interaction between flavonoids apigenin, quercetin, and fisetin with aldehyde dehydrogenase. This is an enzyme that contributes to the acetaldehyde detoxification by oxidizing it to acetate, and also is involved in lipid peroxidation, and metabolism of amino acids, biogenic amines, corticosteroids, retinoids, and protein deglycation. Aldehyde dehydrogenase stability under the action of heat was also investigated and the changes induced by three flavonoids on the conformational stability of the protein were monitored. Spectroscopic studies showed that apigenin, fisetin, and quercetin quenched aldehyde dehydrogenase fluorescence by a dynamic mechanism. Calculating the values of the thermodynamic parameters, it was noticed that the interaction processes between flavonoids and aldehyde dehydrogenase were driven by hydrophobic forces. At the same time, the interaction was enthalpically driven for apigenin, entropically driven for quercetin, and with the same contribution of the enthalpy and entropy for fisetin. The distance between the Trp residues and flavonoids and also the efficiency of the energy transfer between the aldehyde dehydrogenase and flavonoids were evaluated based on FRET. Molecular docking confirmed the results obtained by fluorimetry. Denaturation process of aldehyde dehydrogenase and aldehyde dehydrogenase-flavonoids complexes was investigated. It was observed that apigenin has stabilized protein structure against denaturation, while fisetin and quercetin have a destabilizing effect.
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