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α‐Amylase Inhibitors Based on Thiazolidinone Skeleton: A Promising Approach in Diabetes Management.

Authors :
Singh, Rahul
Sindhu, Jayant
Kumar, Parvin
Hooda, Mona
Aggarwal, Ranjana
Lal, Sohan
Ahmadi, Shahin
Lotfi, Shahram
Singh, Devender
Kumar, Harish
Source :
ChemistrySelect; 12/22/2023, Vol. 8 Issue 48, p1-30, 30p
Publication Year :
2023

Abstract

Thiazolidinone scaffold has become a promising scaffold when it comes to therapeutic importance, and researchers are quite interested in it because of its wide range of applications in the different fields of chemistry. The capacity of this nucleus to interact with a variety of biological targets, including the peroxisome proliferator‐activated receptor (PPAR), protein tyrosine phosphatase 1B, aldose reductase, α‐glucosidase, and α‐amylase, has led to the observation of its antidiabetic effect. α‐Amylase (α‐1,4‐glucan‐4‐glucanohydrolase, EC 3.2.1.1) is one of the most important industrial endoamylases capable of hydrolyzing the internal α‐1,4‐glycosidic bonds in polysaccharides with net retention of α‐anomeric configuration in low molecular weight products, such as glucose, maltose, and maltotriose units. The inhibitors of α‐amylase have the ability to lower endogenous activity, which is crucial for the management of agricultural pests as well as the treatment and prevention of human disorders. In the present review, we attempted to compile the most recent studies on thiazolidinone‐based α‐amylase inhibitors, investigate their therapeutic potential in treating diabetes, comprehend the relationships between structure and activity, offer suggestions for future research and translation of these findings into clinical applications. This comprehensive review strives to be a valuable resource for researchers, medicinal chemists, and healthcare professionals involved in developing and applying novel therapeutics for treating metabolic disorders. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
23656549
Volume :
8
Issue :
48
Database :
Complementary Index
Journal :
ChemistrySelect
Publication Type :
Academic Journal
Accession number :
174881548
Full Text :
https://doi.org/10.1002/slct.202303852