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An Endoperoxide‐Based Hybrid Approach to Deliver Falcipain Inhibitors Inside Malaria Parasites
Author(s) -
Oliveira Rudi,
Newton Ana S.,
Guedes Rita C.,
Miranda Daniela,
Amewu Richard K.,
Srivastava Abhishek,
Gut Jiri,
Rosenthal Philip J.,
O'Neill Paul M.,
Ward Stephen A.,
Lopes Francisca,
Moreira Rui
Publication year - 2013
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201300202
Subject(s) - plasmodium falciparum , cysteine protease , malaria , chloroquine , docking (animal) , biology , protease , vacuole , small molecule , artemisinin , biochemistry , chemistry , enzyme , immunology , medicine , nursing , cytoplasm
Abstract The emergence of artemisinin‐resistant Plasmodium falciparum malaria in Southeast Asia has reinforced the urgent need to discover novel chemotherapeutic strategies to treat and control malaria. To address this problem, we prepared a set of dual‐acting tetraoxane‐based hybrid molecules designed to deliver a falcipain‐2 (FP‐2) inhibitor upon activation by iron(II) in the parasite digestive vacuole. These hybrids are active in the low nanomolar range against chloroquine‐sensitive and chloroquine‐resistant P. falciparum strains. We also demonstrate that in the presence of FeBr 2 or within infected red blood cells, these molecules fragment to release falcipain inhibitors with nanomolar protease inhibitory activity. Molecular docking studies were performed to better understand the molecular interactions established between the tetraoxane‐based hybrids and the cysteine protease binding pocket residues. Our results further indicate that the intrinsic activity of the tetraoxane partner compound can be masked, suggesting that a tetraoxane‐based delivery system offers the potential to attenuate the off‐target effects of known drugs.

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