Binding of flavonoids to yeast aldehyde dehydrogenase: a molecular mechanism and computational approach.
J Biomol Struct Dyn
; 41(20): 11247-11254, 2023 12.
Article
en En
| MEDLINE
| ID: mdl-36571489
ABSTRACT
The interaction of three flavonoids, apigenin, fisetin and quercetin with yeast aldehyde dehydrogenase, ALDH was studied by spectroscopic and molecular docking methods. A combination of both static and dynamic processes interaction mechanism for the binding of flavonoids with ALDH was found. The interaction takes place with moderate binding and the interaction was driven by hydrophobic contacts. The microenvironments of the fluorescent amino acids changed upon flavonoids binding. The distances between ALDH and flavonoids determined by Förster Resonant Energy Transfer (FRET) confirmed the results obtained by fluorescence. The structure of ALDH against thermal denaturation was stabilized by apigenin and destabilized by fisetin and quercetin. Molecular docking simulation showed that all flavonoids bind to the same site of ALDH and confirmed the moderate binding straight found in fluorescence.Communicated by Ramaswamy H. Sarma.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Quercetina
/
Flavonoides
Idioma:
En
Revista:
J Biomol Struct Dyn
Año:
2023
Tipo del documento:
Article
País de afiliación:
Rumanía