Inhibitors of aspartic proteases – potential antimalarial agents

Bibliography

• BOSS C, RICHARD-BILDSTEIN S, WELLER T, FISCHLI W, BINKERT C: Inhibitors of the Plasmodium falciparum parasite aspartic protease plasmepsin II as potential antimalarial agents. Curr. Med. Chem. (2003) 10:883-907.
   PubMed Web of Science ®Google Scholar
• WATERS NC, DOW GS, KOZAR MP: Antimalarial compound identification and design: advances in the patent literature, 2000 – 2003. Expert Opin. Ther. Patents (2004) 14(8):1125-1138.
   Web of Science ®Google Scholar
• BOSS C, RICHARD-BILDSTEIN S, FURNARI R et al.: Inhibitors of plasmepsin II – potential antimalarial agents. Chimia (2004) 58(9):634-639.
   Google Scholar
• RADDING JA: Development of anti-malarial inhibitors of haemoglobinases. Ann. Rep. Med. Chem. (1999) 34:159-168.
   Google Scholar
• WIRTH DF: Malaria: a third world disease in need of first world drug development. Ann. Rep. Med. Chem. (1999) 34:349-358.
   Google Scholar
• WIESNER J, ORTMANN R, JOMAA H, SCHLITZER M: Neue antimalaria-wirkstoffe. Angew. Chem. (2003) 115:5432-5451.
   Google Scholar
• MBAI M, RAJAMANI S, JANUARY CT: Blockade of HERG potassium channels by the antimalarial halofantrine. Circulation (2000) 102(18): Abs 1745.
   Google Scholar
• VENNERSTROM JL, ARBE-BARNES S, BRUN R et al.: Identification of an antimalarial synthetic trioxolane drug development candidate. Nature (2004) 430:900-904.
   PubMed Web of Science ®Google Scholar
• ROSENTHAL PJ: Protease inhibitors. In: Antimalarial Chemotherapy: Mechanisms of Action, Resistance, and New Directions in Drug Discovery. ROSENTHAL PJ (Ed.), Humana Press, Inc., New Jersey, USA (2001):325-345.
   Google Scholar
• JOMAA H, WIESNER J, SANDERBRAND S et al.: Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs. Science (1999) 285:1573-1576.
   PubMed Web of Science ®Google Scholar
• OMARA-OPYENE AL, MOURA PA, SULSONA CR et al.: Genetic disruption of the Plasmodium falciparum digestive vacuole plasmepsins demonstrates their functional redundancy. J. Biol. Chem. (2004) 279(52):54088-54096.
   PubMed Web of Science ®Google Scholar
• LIU J, GLUZMAN IY, DREW ME, GOLDBERG DE: The role of Plasmodium falciparum food vacuole plasmepsins. J. Biol Chem. (2005) 280(2):1432-1437.
   PubMedGoogle Scholar
• SENGE MO, HATSCHER S: The malaria pigment haemozoin – a focal point of action for antimalarial drugs. ChemBioChem. (2000) 1:247-249.
   PubMedGoogle Scholar
• ROBERT A, DECHY-CABARET O, CAZELLES J, MEUNIER B: From mechanistic studies on artemisinin derivatives to new modular antimalarial drugs. Acc. Chem. Res. (2002) 35:167-174.
   PubMed Web of Science ®Google Scholar
• EGAN TJ: Quinoline antimalarials. Expert Opin. Ther. Patents (2001) 11(2):185-209.
   Web of Science ®Google Scholar
• ZIEGLER J, LINCK R, WRIGHT DW: Heme aggregation inhibitors: antimalarial drugs targeting an essential biomineralization process. Curr. Med. Chem. (2001) 8:171-189.
   PubMed Web of Science ®Google Scholar
• BANERJEE R, LIU J, BEATTY W et al.: Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc. Natl. Acad. Sci. USA (2002) 99(2):990-995.
   PubMed Web of Science ®Google Scholar
• ASOJO OA, AFONINA E, GULNIK SV et al.: Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 Å in complex with the inhibitors rs367 and rs370. Acta Cryst. (2002) D58:2001-2008.
   Google Scholar
• PRADE L, JONES AF, BOSS C et al.: X-ray structure of plasmepsin II complexed with a potent achiral inhibitor. J. Biol. Chem. (2005) 280(25):23837-23843.
   PubMedGoogle Scholar
• COOMBS GH, GOLDBERG DE, KLEMBA M, BERRY C, KAY J, MOTTRAM JC: Aspartic proteases of Plasmodium falciparum and other parasitic protozoa as drug targets. Trends Parasitol. (2001) 11:532-537.
   Google Scholar
• SILVA AM, LEE AY, ERICKSON JW, GOLDBERG DE: Structural analysis of plasmepsin II. In: Aspartic Proteinases. James MN (Ed.), Adv. Exp. Med. Biol. Plenum Press, New York, USA (1998) 436:363-373.
   Google Scholar
• MAIBAUM J, FELDMAN DL: Renin inhibitors as novel treatments for cardiovascular disease. Expert Opin. Ther. Patents (2003) 13(5):589-603.
   Web of Science ®Google Scholar
• DEISS LP, GALINKA H, BERISSI H, COHEN O, KIMCHI A: Cathepsin D protease mediates programmed cell death induced by interferon-γ, Fas/APO-1 and TNF-α. EMBO J. (1996) 15:3861-3870.
   PubMed Web of Science ®Google Scholar
• MUELLER R, HUERZELER M, BOSS C: Synthesis of plasmepsin II inhibitors – potential antimalarial agents. Molecules (2003) 8:556-564.
   Google Scholar
• DESJARDIN RE, CANFIELD CJ, HAYNES JD, CHULAY JD: Quantitative assessment of antimalarial activity in vitro by semiautomated microdilution technique. Antimicrob. Agents Chemother. (1979) 16:710-718.
   PubMed Web of Science ®Google Scholar
• CARCACHE DA, HOERTNER SR, BERTOGG A et al.: De novo design, synthesis, and in vitro evaluation of a new class of nonpeptidic inhibitors of the malarial enzyme plasmepsin II. ChemBioChem (2002):1137-1141.
   PubMedGoogle Scholar
• CARCACHE DA, HOERTNER SR, BERTOGG A et al.: A new class of inhibitors for the malarial aspartic protease plasmepsin II based on a central 11-azatricyclo[6.2.1.027]undeca-2,4,6-triene scaffold. Helv. Chim. Acta (2003) 86:2192-2209.
   Google Scholar
• CARCACHE DA, HOERTNER SR, SEILER P: Development of a new class of inhibitors for the malarial aspartic protease plasmepsin II based on a central 7-azabicyclo[2.2.1]heptane scaffold. Helv. Chim. Acta (2003) 86:2173-2191.
   Google Scholar
• HOF F, DIEDERICH F: Medicinal chemistry in academia: molecular recognition with biological receptors. Chem. Comm. (2004) 5:484-487.
   Google Scholar
• OEFNER C, BINGGELI A, BREU V et al.: Renin inhibition by substituted piperidines: a novel paradigm for the inhibition of monomeric aspartic proteinases? Chem Biol. (1999) 6(3):127-31.
   PubMed Web of Science ®Google Scholar
• HAQUE TS, SKILLMAN AG, LEE CE et al.: Potent low-molecular-weight non-peptide inhibitors of malarial aspartyl protease plasmepsin II. J. Med. Chem. (1999) 42:1428-1440.
   PubMed Web of Science ®Google Scholar
• MALY DJ, HUANG L, ELLMAN JA: Combinatorial strategies for targeting protein families: application to the proteases. ChemBioChem (2002):16-37.
   PubMedGoogle Scholar
• ASOJO OA, GULNIK SV, AFONINA E et al.: Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum. J. Mol. Biol. (2003) 327:173-181.
   PubMedGoogle Scholar
• BRINNER KM, KIM JM, HABASHITA H, GLUZMAN IY, GOLDBERG DE, ELLMAN JA: Novel and potent anti-malarial agents. Bioorg. Med. Chem. (2002) 10:3649-3661.
   PubMedGoogle Scholar
• CARROLL CD, PATEL H, JOHNSON O et al.: Identification of potent inhibitors of Plasmodium falciparum plasmepsin II from an encoded statine combinatorial library. Bioorg. Med. Chem. Lett. (1998) 8:2315-2320.
   PubMedGoogle Scholar
• CARROLL CD, JOHNSON TO, TAO S et al.: Evaluation of a structure-based statine cyclic diamino amide encoded combinatorial library against plasmepsin II and cathepsin D. Bioorg. Med. Chem. Lett. (1998) 8:3203-3206.
   PubMedGoogle Scholar
• KISO A, HIDAKA K, KIMURA T et al.: Substrate transition-state analogue inhibitors of plasmepsin II as antimalarial drugs. Peptide Science (2002):297-300.
   PubMedGoogle Scholar
• NEZAMI A: Structure-based design of novel inhibitors of plasmepsins: a family of antimalarial targets. PhD thesis, Johns Hopkins University (2003) UMI Number: 3107552.
   Google Scholar
• NEZAMI A, KIMURA T, HIDAKA K et al.: High-affinity inhibition of a family of Plasmodium falicparum proteases by a designed adaptive inhibitor. Biochemistry (2003) 42:8459-8464.
   PubMed Web of Science ®Google Scholar
• ABDEL-RAHMAN HM, KIMURA T, HIDAKA K et al.: Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases. Biol. Chem. (2004) 385:1035-1039.
   PubMed Web of Science ®Google Scholar
• KISO A, HIDAKA K, KIMURA T et al.: Search for substrate-based inhibitors fitting the s2′ space of malarial aspartic protease plasmepsin II. J. Peptide Sci. (2004) 10:641-647.
   PubMedGoogle Scholar
• ERSMARK K, NERVALL M, HAMELINK E et al.: Synthesis of malarial plasmepsin inhibitors and predicition of binding modes by molecular dynamics simulations. J. Med. Chem. (2005) 48:6090-6106.
   PubMed Web of Science ®Google Scholar
• ERSMARK K, FEIERBERG I, BJELIC S et al.: Potent inhibitors of the Plasmodium falciparum enzymes plasmepsin I and II devoid of cathepsin D inhibitory activity. J. Med. Chem. (2004) 47:110-122.
   PubMed Web of Science ®Google Scholar
• ERSMARK K, FEIERBERG I, BJELIC S et al.: C2-Symmetric inhibitors of Plasmodium falciparum plasmepsin II: synthesis and theoretical predicitions. Bioorg. Med. Chem. (2003) 11:3723-3733.
   PubMedGoogle Scholar
• OSCARSSON K, OSCARSON S, VRANG L, HAMELINK E, HALLBERG A, SAMUELSSON B: New potent C2-symmetric malaria plasmepsin I and II inhibitors. Bioorg. Med. Chem. (2003) 11:1235-1246.
   PubMedGoogle Scholar
• JOHANSSON PO, LINDBERG J, BLACKMAN MJ et al.: Design and synthesis of potent inhibitors of plasmepsin I and II: X-ray crystal structure of inhibitor in complex with plasmepsin II. J. Med. Chem. (2005) 48:4400-4409.
   PubMedGoogle Scholar
• JOHANSSON PO, CHEN Y, BELFRAGE AK et al.: Design and synthesis of potent inhibitors of the malaria aspartyl proteases plasmepsin I and II. Use of solid-phase synthesis to explore novel statine motifs. J. Med. Chem. (2004) 47:3353-3366.
   PubMed Web of Science ®Google Scholar