ArticleMolecules (Basel, Switzerland)2016
Synthesis of N-(6-Arylbenzo[d]thiazole-2-acetamide Derivatives and Their Biological Activities: An Experimental and Computational Approach.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 43 citations in OpenAlex.
- Review
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- Pyridylpiperazine-based carbodithioates as urease inhibitors: synthesis and biological evaluation.Frontiers in chemistry · 2024Article
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- Antiurease screening of alkyl chain-linked thiourea derivatives:RSC advances · 2022Article
- Identification of novel bacterial urease inhibitors through molecular shape and structure based virtual screening approaches.RSC advances · 2020Article
- Design, synthesis, and biological evaluation of novelBMC chemistry · 2019Article
- A review on the development of urease inhibitors as antimicrobial agents against pathogenic bacteria.Journal of advanced research · 2018Review
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Authors and funding
10 authors at 7 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
A new series of N-(6-arylbenzo[d]thiazol-2-yl)acetamides were synthesized by C-C coupling methodology in the presence of Pd(0) using various aryl boronic pinacol ester/acids. The newly synthesized compounds were evaluated for various biological activities like antioxidant, haemolytic, antibacterial and urease inhibition. In bioassays these compounds were found to have moderate to good activities. Among the tested biological activities screened these compounds displayed the most significant activity for urease inhibition. In urease inhibition, all compounds were found more active than the standard used. The compound N-(6-(p-tolyl)benzo[d]thiazol-2-yl)acetamide was found to be the most active. To understand this urease inhibition, molecular docking studies were performed. The in silico studies showed that these acetamide derivatives bind to the non-metallic active site of the urease enzyme. Structure-activity studies revealed that H-bonding of compounds with the enzyme is important for its inhibition.
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