Investigation of inhibitory properties of some hydrazone compounds on hCA I, hCA II and AChE enzymes.
Acetylcholinesterase
/ metabolism
Carbonic Anhydrase I
/ antagonists & inhibitors
Carbonic Anhydrase II
/ antagonists & inhibitors
Carbonic Anhydrase Inhibitors
/ chemical synthesis
Cholinesterase Inhibitors
/ chemical synthesis
Dose-Response Relationship, Drug
Humans
Hydrazones
/ chemical synthesis
Molecular Structure
Structure-Activity Relationship
Acetylcholinesterase
Carbonic anhydrase
Enzyme inhibition
Hydrazone
Mannich base
Journal
Bioorganic chemistry
ISSN: 1090-2120
Titre abrégé: Bioorg Chem
Pays: United States
ID NLM: 1303703
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
05
12
2018
revised:
28
01
2019
accepted:
03
02
2019
pubmed:
12
2
2019
medline:
14
4
2020
entrez:
12
2
2019
Statut:
ppublish
Résumé
Recently, inhibition of carbonic anhydrase (hCA) and acetylcholinesterase (AChE) have appeared as a promising approach for pharmacological intervention in a variety of disorders such as glaucoma, epilepsy, obesity, cancer, and Alzheimer's disease. Keeping this in mind, N,N'-bis[(1-aryl-3-heteroaryl)propylidene]hydrazine dihydrochlorides, N1-N11, P1, P4-P8, and R1-R6, were synthesized to investigate their inhibitory activity against hCA I, hCA II, and AChE enzymes. All compounds in N, P, and R-series inhibited hCAs (I and II) and AChE more efficiently than the reference compounds acetazolamide (AZA), and tacrine. According to the activity results, the most effective inhibitory compounds were in R-series with the K
Identifiants
pubmed: 30743172
pii: S0045-2068(18)31417-2
doi: 10.1016/j.bioorg.2019.02.008
pii:
doi:
Substances chimiques
Carbonic Anhydrase Inhibitors
0
Cholinesterase Inhibitors
0
Hydrazones
0
Acetylcholinesterase
EC 3.1.1.7
Carbonic Anhydrase I
EC 4.2.1.-
Carbonic Anhydrase II
EC 4.2.1.-
CA2 protein, human
EC 4.2.1.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
316-321Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.