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pubmed-article:16054370pubmed:abstractTextThe increasing resistance of the malarial parasite to antimalarial drugs is a major contributor to the reemergence of the disease and increases the need for new drug targets. The two aspartic proteases, plasmepsins I and II, from Plasmodium falciparum have recently emerged as potential targets. In an effort to inhibit these hemoglobinases, a series of inhibitors encompassing a basic hydroxyethylamine transition state isostere as a central fragment were prepared. The synthesized compounds were varied in the P1' position and exhibited biological activities in the range of 31 to >2000 nM. To try to rationalize the results, molecular docking and 3D-QSAR analysis were used.lld:pubmed
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pubmed-article:16054370pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:16054370pubmed:articleTitleSynthesis, biological evaluation, and modeling studies of inhibitors aimed at the malarial proteases plasmepsins I and II.lld:pubmed
pubmed-article:16054370pubmed:affiliationDepartment of Medicinal Chemistry, Uppsala University, Box 574, SE-751 23 Uppsala, Sweden.lld:pubmed
pubmed-article:16054370pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16054370pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed