3 years ago

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

Maria J. Alves, Hamadeh Tarazi, Muhammad Yar, Ather Farooq Khan, Ayesha Babar, Vera Duarte, Mohammed B. Alshammari, Munawwar Ali Munawwar, Haffsah Iqbal, Mazhar Amjad Gilani


This study describes an efficient synthesis of a series of novel ethyl 2-[aryl(thiazol-2-yl)amino]acetates (4al) from N-arylthiazole-2-amines (3al). 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. α-glucosidase and β-glucosidase inhibition activities of N-arylthiazole-2-amines (3al) and ethyl 2-[aryl(thiazol-2-yl)amino]acetates (4al) 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 α-glucosidase having IC50 value of 150.4 ± 1.9 μM which was almost two folds as compared to acarbose (336.9 ± 9.0 μM) 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.

Publisher URL: https://link.springer.com/article/10.1007/s00044-017-2018-3

DOI: 10.1007/s00044-017-2018-3

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.