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Anti-malarial drug development using models of enzyme structure.
Li, Z; Chen, X; Davidson, E; Zwang, O; Mendis, C; Ring, C S; Roush, W R; Fegley, G; Li, R; Rosenthal, P J.
Afiliación
  • Li Z; Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
Chem Biol ; 1(1): 31-7, 1994 Sep.
Article en En | MEDLINE | ID: mdl-9383368
BACKGROUND: The trophozoite stage of the malaria parasite infects red blood cells. During this phase of their life-cycle, the parasites use hemoglobin as their principal source of amino acids, using a cysteine protease to degrade it. We have previously reported a three-dimensional model of this cysteine protease, based on the structures of homologous proteases, and the use of the program DOCK to identify a ligand for the malaria protease. RESULTS: Here we describe the design of improved ligands starting from this lead. Ligand design was based on the predicted configuration of the lead compound docked to the model three-dimensional structure of the protease. The lead compound has an IC50 of 6 microM, and our design/synthesis strategy has resulted in increasingly potent derivatives that block the ability of the parasites to infect and/or mature in red blood cells. The two best derivatives to date have IC50(s) of 450 nM and 150 nM. CONCLUSIONS: A new class of anti-malarial chemotherapeutics has resulted from a computational search that was based on a model of the target protease. Despite the lack of a detailed experimental structure of the target enzyme or the enzyme-inhibitor complex, we have been able to identify compounds with increased potency. These compounds approach the activity of chloroquine (IC50 = 20 nM), but have a distinct mechanism of action. This series of compounds could thus lead to new therapies for chloroquine-resistant malaria.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Plasmodium / Enzimas / Antimaláricos Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Chem Biol Asunto de la revista: BIOLOGIA / BIOQUIMICA / QUIMICA Año: 1994 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Plasmodium / Enzimas / Antimaláricos Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Chem Biol Asunto de la revista: BIOLOGIA / BIOQUIMICA / QUIMICA Año: 1994 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos