Inhibitory mechanism of clioquinol and its derivatives at the exopeptidase site of human angiotensin-converting enzyme-2 and receptor binding domain of SARS-CoV-2 viral spike.
SARS-CoV-2
clioquinol and its derivatives
exopeptidase
molecular dynamic simulation
receptor binding domain
Journal
Journal of biomolecular structure & dynamics
ISSN: 1538-0254
Titre abrégé: J Biomol Struct Dyn
Pays: England
ID NLM: 8404176
Informations de publication
Date de publication:
04 2023
04 2023
Historique:
medline:
13
4
2023
pubmed:
1
3
2022
entrez:
28
2
2022
Statut:
ppublish
Résumé
The outbreak of SARS-CoV-2 infections around the world has prompted scientists to explore different approaches to develop therapeutics against COVID-19. This study focused on investigating the mechanism of inhibition of clioquinol (CLQ) and its derivatives (7-bromo-5-chloro-8-hydroxyquinoline (CLBQ), 5, 7-Dichloro-8-hydroxyquinoline (CLCQ)) against the viral glycoprotein, and human angiotensin-converting enzyme-2 (hACE-2) involved in SARS-CoV-2 entry. The drugs were docked at the exopeptidase site of hACE-2 and receptor binding domain (RBD) sites of SARS-CoV-2 S
Identifiants
pubmed: 35220925
doi: 10.1080/07391102.2022.2043938
doi:
Substances chimiques
Clioquinol
7BHQ856EJ5
Exopeptidases
EC 3.4.-
Angiotensins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
2992-3001Subventions
Organisme : NIMHD NIH HHS
ID : U54 MD007605
Pays : United States