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Issue 36, 2016
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Targeting of the Leishmania mexicana cysteine protease CPB2.8ΔCTE by decorated fused benzo[b]thiophene scaffold

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Abstract

A potent and highly selective anhydride-based inhibitor of Leishmania mexicana cysteine protease CPB2.8ΔCTE (IC50 = 3.7 μM) was identified. The details of the interaction of the ligand with the enzyme active site were investigated by NMR biomimetic experiments and docking studies. Results of inhibition assays, NMR and theoretical studies indicate that the ligand acts initially as a non-covalent inhibitor and later as an irreversible covalent inhibitor by chemoselective attack of CYS 25 thiolate to an anhydride carbonyl.

Graphical abstract: Targeting of the Leishmania mexicana cysteine protease CPB2.8ΔCTE by decorated fused benzo[b]thiophene scaffold

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Publication details

The article was received on 02 Mar 2016, accepted on 09 Mar 2016 and first published on 11 Mar 2016


Article type: Paper
DOI: 10.1039/C6RA05557E
Citation: RSC Adv., 2016,6, 30628-30635
  • Open access: Creative Commons BY license
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    Targeting of the Leishmania mexicana cysteine protease CPB2.8ΔCTE by decorated fused benzo[b]thiophene scaffold

    A. Scala, N. Micale, A. Piperno, A. Rescifina, T. Schirmeister, J. Kesselring and G. Grassi, RSC Adv., 2016, 6, 30628
    DOI: 10.1039/C6RA05557E

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