Molecular docking and glucosidase inhibition studies of novel N-arylthiazole-2-amines and Ethyl 2-[aryl(thiazol-2-yl)amino]acetates

• Type: Article in International Scientific Journal
• Date: 2017

Authors

Babar, A (Author) Other; Yar, M (Author) Other; Tarazi, H (Author) Other; Duarte, V (Author) FEUP; Alshammari, MB (Author) Other; Gilani, MA (Author) Other; Iqbal, H (Author) Other; Munawwar, MA (Author) Other; Alves, MJ (Author) Other; Khan, AF (Author) Other

Journal

Title: Medicinal Chemistry Research

Vol. 26

Pages: 3247-3261

ISSN: 1054-2523

Publisher: Springer Nature

Indexing

ISI Web of Knowledge - 3 Citations

Scopus - 4 Citations

Other information

Authenticus ID: P-00M-XR4

DOI: 10.1007/s00044-017-2018-3

Abstract (EN): This study describes an efficient synthesis of a series of novel ethyl 2-[aryl(thiazol-2-yl)amino]acetates (4a-l) from N-arylthiazole-2-amines (3a-l). The reaction conditions were optimized and the best results were obtained when ethyl chloroacetate was used as alkylating agent and NaH as base in THF. alpha-glucosidase and beta-glucosidase inhibition activities of N-arylthiazole-2-amines (3a-l) and ethyl 2-[aryl(thiazol-2-yl)amino]acetates (4a-l) were determined, which revealed that most of the compounds showed high percentage inhibition towards the enzymes. Among the synthesized compounds, 4e appeared to have the highest inhibition towards alpha-glucosidase having IC50 value of 150.4 +/- 1.9 mu M which was almost two folds as compared to acarbose (336.9 +/- 9.0 mu M) taken as standard. Molecular docking of the compounds 3g, 3f, 4a, and 4e was also performed which showed their bonding modes to the enzyme's active sites via amino and acetate groups, respectively.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 15