Thermodynamic and functional changes of alpha-chymotrypsin after interaction with gallic acid.
Gallic acid
MD simulation
Molecular interaction
Spectroscopy
α-Chymotrypsin
Journal
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy
ISSN: 1873-3557
Titre abrégé: Spectrochim Acta A Mol Biomol Spectrosc
Pays: England
ID NLM: 9602533
Informations de publication
Date de publication:
03 Mar 2024
03 Mar 2024
Historique:
received:
31
10
2023
revised:
24
02
2024
accepted:
02
03
2024
medline:
7
3
2024
pubmed:
7
3
2024
entrez:
6
3
2024
Statut:
aheadofprint
Résumé
In the present study, the interaction mechanism between gallic acid (GA) and α-Chymotrypsin (α-CT) was investigated by employing a series ofspectroscopic methods, computational docking and molecular dynamic (MD) simulation. Fluorescence spectra analysis indicated the formation of a stable complex between GA and α-CT, where the quenching of the fluorescence emission was predominantly characterized by a static mechanism. TheCA obtained binding constants for the α-CT-GA complex were in the order of 10
Identifiants
pubmed: 38447443
pii: S1386-1425(24)00275-0
doi: 10.1016/j.saa.2024.124109
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
124109Informations de copyright
Copyright © 2024 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.