| Literature DB >> 28763614 |
Santo Previti1, Roberta Ettari1, Sandro Cosconati2, Giorgio Amendola2, Khawla Chouchene3, Annika Wagner4,5, Ute A Hellmich4,5, Kathrin Ulrich6, R Luise Krauth-Siegel6, Peter R Wich7, Ira Schmid7, Tanja Schirmeister7, Jiri Gut8, Philip J Rosenthal8, Silvana Grasso1, Maria Zappalà1.
Abstract
This paper describes the development of a class of peptide-based inhibitors as novel antitrypanosomal and antimalarial agents. The inhibitors are based on a characteristic peptide sequence for the inhibition of the cysteine proteases rhodesain of Trypanosoma brucei rhodesiense and falcipain-2 of Plasmodium falciparum. We exploited the reactivity of novel unsaturated electrophilic functions such as vinyl-sulfones, -ketones, -esters, and -nitriles. The Michael acceptors inhibited both rhodesain and falcipain-2, at nanomolar and micromolar levels, respectively. In particular, the vinyl ketone 3b has emerged as a potent rhodesain inhibitor (k2nd = 67 × 106 M-1 min-1), endowed with a picomolar binding affinity (Ki = 38 pM), coupled with a single-digit micromolar activity against Trypanosoma brucei brucei (EC50 = 2.97 μM), thus being considered as a novel lead compound for the discovery of novel effective antitrypanosomal agents.Entities:
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Year: 2017 PMID: 28763614 DOI: 10.1021/acs.jmedchem.7b00405
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446