Biochemical and computational insights of adenosine deaminase inhibition by Epigallocatechin gallate.
Adenosine deaminase
Epigallocatechin gallate
Fluorescence spectroscopy
ITC
Molecular dynamics
Journal
Computational biology and chemistry
ISSN: 1476-928X
Titre abrégé: Comput Biol Chem
Pays: England
ID NLM: 101157394
Informations de publication
Date de publication:
Dec 2019
Dec 2019
Historique:
received:
06
08
2018
revised:
12
08
2019
accepted:
14
08
2019
pubmed:
25
8
2019
medline:
20
12
2019
entrez:
25
8
2019
Statut:
ppublish
Résumé
Epigallocatechin gallate, a flavonoid from Camellia sinensis possess various pharmacological activities such as anticancer, antimicrobial and antioxidant etc. Adenosine deaminase, (ADA), is a key enzyme involved in the purine metabolism, the inhibitors of which is being considered as highly promising candidate for the development of anti-proliferative and anti-inflammatory drugs. In this work we studied adenosine deaminase inhibitory activity of epigallocatechin gallate by using biophysical and computational methods. The enzyme inhibition study result indicated that epigallocatechin gallate possess strong inhibitory activity on ADA. ITC study revealed the energetics of binding. Also the binding is confirmed by using fluorescence spectroscopy. The structural details of binding are obtained from molecular docking and MD simulation studies.
Identifiants
pubmed: 31445420
pii: S1476-9271(18)30567-X
doi: 10.1016/j.compbiolchem.2019.107111
pii:
doi:
Substances chimiques
Adenosine Deaminase Inhibitors
0
Catechin
8R1V1STN48
epigallocatechin gallate
BQM438CTEL
Adenosine Deaminase
EC 3.5.4.4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
107111Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.