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Design and synthesis of 2-substituted-5-(4-trifluoromethylphenyl-sulphonamido)benzoxazole derivatives as human GST P1-1 inhibitors
Stockholm University, Faculty of Science, Department of Neurochemistry.
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Number of Authors: 7
2018 (English)In: Artificial Cells, Nanomedicine, and Biotechnology, ISSN 2169-1401, Vol. 46, no 3, p. 510-517Article in journal (Refereed) Published
Abstract [en]

The glutathione transferases (GSTs) are a family of widely distributed Phase II detoxification enzymes. GST P1-1 is frequently overexpressed in rat and human tumours. It is suggested that overexpression of hGST P1-1 by human tumor cells may play a role in resistance to cancer chemotherapy. Hence, hGST P1-1 can be a promising target for cancer treatment. In this study, new hGST P1-1 inhibitors, 2-(4-substitutedphenyl/benzyl)-5-(4-trifluoromethylphenylsulphonamido) benzoxazole derivatives (Va-Vk) have been designed and synthesized. Surprisingly, in vitro hGST P1-1 enzyme inhibition studies demonstrated that all of the tested compounds except Vj had better activity than the reference drug EA and it is also correlated with the docking results. Additionally we compared the interactions with hGST P1-1 enzyme of newly synthesized compound Vh (bearing CF3 group) and previously synthesized compound 5f (bearing NO2 group). According to the docking results, compound Vh bound to the hGST P1-1 enzyme with a higher affinity compared to 5f. Therefore, we can consider that these data make a sense and can explain its higher activity. The compounds that obtained from this research could be used as scaffolds in design of new potent hGST P1-1 inhibitors useful in the treatment of the resistance of cancer chemotherapy.

Place, publisher, year, edition, pages
2018. Vol. 46, no 3, p. 510-517
Keyword [en]
Benzoxazole, heterocyclic synthesis, human glutathione transferase P1-1, inhibitory activity, molecular docking, sulphonamide
National Category
Medicinal Chemistry Pharmacology and Toxicology Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-154661DOI: 10.1080/21691401.2017.1324464ISI: 000427659400008PubMedID: 28503938OAI: oai:DiVA.org:su-154661DiVA, id: diva2:1202066
Available from: 2018-04-27 Created: 2018-04-27 Last updated: 2018-04-27Bibliographically approved

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Bolelli, KayhanMusdal, YamanMannervik, Bengt
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