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Peptidic boronic acids are potent cell-permeable inhibitors of the malaria parasite egress serine protease SUB1

Elīna Līdumniece, Chrislaine Withers‐Martinez, Fiona Hackett, Christine R. Collins, Abigail J. Perrin, Konstantinos Koussis, C. Bisson, Michael J. Blackman, Aigars Jirgensons

2021Proceedings of the National Academy of Sciences29 citationsDOIOpen Access PDF

Abstract

Significance Malaria remains a major global health threat. In the face of increasing resistance to available chemotherapeutics, new antimalarial drugs with new modes of action are urgently needed. The causative agent of malaria is a single-celled parasite that invades and replicates within red blood cells. Escape from the red cell, a process called egress, involves a proteolytic pathway triggered by an essential parasite subtilisin-like serine protease called SUB1. Here, we describe the development and rational optimization of a potent, membrane-permeable substrate-based boronic acid compounds that block egress and parasite proliferation by direct inhibition of SUB1 activity. The compounds could form the basis of a new type of antimalarial medicine that would both protect against infection and treat disease.

Topics & Concepts

Serine proteaseMalariaMASP1Parasite hostingProteaseSerinePlasmodium falciparumBiochemistryChemistryBiologyEnzymeImmunologyComputer scienceWorld Wide WebMalaria Research and ControlInsect Resistance and GeneticsMosquito-borne diseases and control
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