Synthetic α-glucosidase inhibitors as promising anti-diabetic agents: Recent developments and future challenges.
Diabetes mellitus
Heterocyclic
Structure-activity relationship (SAR)
Synthetic
α-Glucosidase inhibitors
Journal
European journal of medicinal chemistry
ISSN: 1768-3254
Titre abrégé: Eur J Med Chem
Pays: France
ID NLM: 0420510
Informations de publication
Date de publication:
05 Mar 2023
05 Mar 2023
Historique:
received:
21
11
2022
revised:
06
01
2023
accepted:
11
01
2023
pubmed:
22
1
2023
medline:
25
2
2023
entrez:
21
1
2023
Statut:
ppublish
Résumé
Diabetes mellitus is one of the biggest challenges for the scientific community in the 21st century. It is a well-recognized multifactorial health problem contributes significantly to high mortality rates by causing serious health complications mainly related to cardiovascular diseases, kidney damage and neuropathy. The inhibition of α-glucosidase (enzyme that catalyses starch hydrolysis in the intestine) is an effective therapeutic approach for controlling hyperglycemia associated with type-2 diabetes. However, the presently approved drugs/inhibitors such as acarbose, miglitol and voglibose have several undesirable gastrointestinal side effects impeding their applications. Therefore, search for novel and more effective inhibitors with reduced side effects and less cost remains a fascinating area of research. In this context, a large variety of α-glucosidase inhibitors have been identified in recent years that demands attention from drug development community. This review is therefore an effort to summarize and highlight the promising α-glucosidase inhibitors especially those which are primarily based on aromatic heterocyclic scaffolds such as coumarin, imidazole, isatin, pyrimidine, quinazoline, triazine, thiazole etc, having improved safety and pharmacological profiles.
Identifiants
pubmed: 36680985
pii: S0223-5234(23)00034-X
doi: 10.1016/j.ejmech.2023.115119
pii:
doi:
Substances chimiques
Glycoside Hydrolase Inhibitors
0
Hypoglycemic Agents
0
Acarbose
T58MSI464G
alpha-Glucosidases
EC 3.2.1.20
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
115119Informations de copyright
Copyright © 2023 Elsevier Masson SAS. 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.