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Facile benzothiazole-triazole based thiazole derivatives as novel thymidine phosphorylase and α-glucosidase inhibitors: Experimental and computational approaches.

Authors :
Khan S
Hussain R
Khan Y
Iqbal T
Ullah F
Felemban S
Khowdiary MM
Source :
Enzyme and microbial technology [Enzyme Microb Technol] 2024 Sep; Vol. 179, pp. 110470. Date of Electronic Publication: 2024 Jun 13.
Publication Year :
2024

Abstract

The present study reports the new thiazole (A-L) derivatives based on benzothiazole fused triazole which were synthesized and assessed against thymidine phosphorylase and α-glucosidase enzymes. Several compounds with the same basic structure but different substituents were found to have high activity against the targeted enzymes, while others with the same basic skeleton but different substituents were found to have medium to low activity among the members of tested series. These analogs showed a varied range of inhibition in both case thymidine phosphorylase and alpha glucosidase, A (IC <subscript>50</subscript> = 7.20 ± 0.30 µM and IC <subscript>50</subscript> = 1.30 ± 0.70 µM), B (IC <subscript>50</subscript> = 8.80 ± 0.10 µM and IC <subscript>50</subscript> = 2.10 ± 0.30 µM), C (IC <subscript>50</subscript> = 8.90 ± 0.40 µM and IC <subscript>50</subscript> = 3.20 ± 0.20 µM) and thiazole containing analogs such as G (IC <subscript>50</subscript> = 11.10 ± 0.20 µM and IC <subscript>50</subscript> = 7.80 ± 0.20 µM) and H (IC <subscript>50</subscript> = 12.30 ± 0.30 µM and IC <subscript>50</subscript> = 6.30 ± 0.20 µM). When compared with standard drugs 7-Deazaxanthine, 7DX (IC <subscript>50</subscript> = 10.60 ± 0.50 µM) and acarbose (IC <subscript>50</subscript> = 4.30 ± 0.30 µM) respectively. These analogs were also subjected to molecular docking studies which indicated the binding interaction of molecules with active sites of the enzyme and strengthen the drug profile of these compounds. ADMET studies also predict the drug-like properties of these compounds, with no violations of drug likeness rules.<br /> (Copyright © 2024 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1879-0909
Volume :
179
Database :
MEDLINE
Journal :
Enzyme and microbial technology
Publication Type :
Academic Journal
Accession number :
38917733
Full Text :
https://doi.org/10.1016/j.enzmictec.2024.110470