메뉴 건너뛰기




Volumn 50, Issue 24, 2007, Pages 6024-6031

Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMALARIAL AGENT; BESTATIN; CHLOROQUINE; CYTOSOL AMINOPEPTIDASE; DIPEPTIDE DERIVATIVE; EXOPEPTIDASE; HEMOGLOBIN; LEUCINE; PHENYLALANINE; PHOSPHINE DERIVATIVE;

EID: 37849041347     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm070733v     Document Type: Article
Times cited : (88)

References (29)
  • 1
    • 0034972445 scopus 로고    scopus 로고
    • The ears of the hippopotamus: Manifestations, determinants, and estimates of the malaria burden
    • 1-2 Suppl, 1-11
    • Breman, J. G. The ears of the hippopotamus: Manifestations, determinants, and estimates of the malaria burden. Am. J. Trop. Med. Hyg. 2001, 64 (1-2 Suppl), 1-11.
    • (2001) Am. J. Trop. Med. Hyg , vol.64
    • Breman, J.G.1
  • 2
    • 2342623947 scopus 로고    scopus 로고
    • Roll Back Malaria: A failing global health campaign
    • Yamey, G. Roll Back Malaria: A failing global health campaign. BMJ [Br. Med. J.] 2004, 328 (7448), 1086-7.
    • (2004) BMJ [Br. Med. J.] , vol.328 , Issue.7448 , pp. 1086-1087
    • Yamey, G.1
  • 3
    • 33644978572 scopus 로고    scopus 로고
    • Overexpression, of leucyl aminopeptidase in Plasmodium falciparum parasites. Target for the antimalarial activity of bestatin
    • Gardiner, D. L.; Trenholme, K. R.; Skinner-Adams, T. S.; Stack, C. M.; Dalton, J. P.; Overexpression, of leucyl aminopeptidase in Plasmodium falciparum parasites. Target for the antimalarial activity of bestatin. J. Biol. Chem. 2006, 281 (3), 1741-5.
    • (2006) J. Biol. Chem , vol.281 , Issue.3 , pp. 1741-1745
    • Gardiner, D.L.1    Trenholme, K.R.2    Skinner-Adams, T.S.3    Stack, C.M.4    Dalton, J.P.5
  • 4
    • 0036183460 scopus 로고    scopus 로고
    • Hydrolysis of erythrocyte proteins by proteases of malaria parasites
    • Rosenthal, P. J. Hydrolysis of erythrocyte proteins by proteases of malaria parasites. Curr. Opin. Hematol. 2002, 9 (2), 140-5.
    • (2002) Curr. Opin. Hematol , vol.9 , Issue.2 , pp. 140-145
    • Rosenthal, P.J.1
  • 6
    • 0038115341 scopus 로고    scopus 로고
    • The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity
    • Grembecka, J.; Mucha, A.; Cierpicki, T.; Kafarski, P. The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity. J. Med. Chem. 2003, 46 (13), 2641-55.
    • (2003) J. Med. Chem , vol.46 , Issue.13 , pp. 2641-2655
    • Grembecka, J.1    Mucha, A.2    Cierpicki, T.3    Kafarski, P.4
  • 7
    • 0020476095 scopus 로고
    • Avidin is a slow-binding inhibitor of pyruvate carboxylase
    • Duggleby, R. G.; Attwood, P. V.; Wallace, J. C.; Keech, D. B. Avidin is a slow-binding inhibitor of pyruvate carboxylase. Biochemistry 1982, 21 (14), 3364-70.
    • (1982) Biochemistry , vol.21 , Issue.14 , pp. 3364-3370
    • Duggleby, R.G.1    Attwood, P.V.2    Wallace, J.C.3    Keech, D.B.4
  • 8
    • 0026602711 scopus 로고
    • Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin
    • Burley, S. K.; David, P. R.; Sweet, R. M.; Taylor, A.; Lipscomb, W. N. Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. J. Mol. Biol. 1992, 224 (1), 113-40.
    • (1992) J. Mol. Biol , vol.224 , Issue.1 , pp. 113-140
    • Burley, S.K.1    David, P.R.2    Sweet, R.M.3    Taylor, A.4    Lipscomb, W.N.5
  • 9
    • 0027237615 scopus 로고
    • X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: Formulation of a catalytic mechanism featuring a gem- diolate transition state
    • Kim, H.; Lipscomb, W. N. X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: Formulation of a catalytic mechanism featuring a gem- diolate transition state. Biochemistry 1993, 32 (33), 8465-78.
    • (1993) Biochemistry , vol.32 , Issue.33 , pp. 8465-8478
    • Kim, H.1    Lipscomb, W.N.2
  • 10
    • 0029116127 scopus 로고
    • Transition state analogue L-leucine-phosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new crystal form
    • Strater, N.; Lipscomb, W. N. Transition state analogue L-leucine-phosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new crystal form. Biochemistry 1995, 34 (28), 9200-10.
    • (1995) Biochemistry , vol.34 , Issue.28 , pp. 9200-9210
    • Strater, N.1    Lipscomb, W.N.2
  • 11
    • 33745041171 scopus 로고    scopus 로고
    • Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems
    • Liu, J.; Istvan, E. S.; Gluzman, I. Y.; Gross, J.; Goldberg, D. E. Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems. Proc. Natl. Acad. Sci. U.S.A. 2006, 103 (23), 8840-5.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , Issue.23 , pp. 8840-8845
    • Liu, J.1    Istvan, E.S.2    Gluzman, I.Y.3    Gross, J.4    Goldberg, D.E.5
  • 12
    • 0034844897 scopus 로고    scopus 로고
    • The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes
    • Gavigan, C. S.; Dalton, J. P.; Bell, A. The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes. Mol. Biochem. Parasitol. 2001, 117 (1), 37-48.
    • (2001) Mol. Biochem. Parasitol , vol.117 , Issue.1 , pp. 37-48
    • Gavigan, C.S.1    Dalton, J.P.2    Bell, A.3
  • 13
    • 0030610839 scopus 로고    scopus 로고
    • Cellular uptake of 3H-bestatin in tissues of mice after its intravenous injection
    • Scornik, O. A.; Botbol, V. Cellular uptake of 3H-bestatin in tissues of mice after its intravenous injection. Drug Metab. Dispos. 1997, 25 (7), 798-804.
    • (1997) Drug Metab. Dispos , vol.25 , Issue.7 , pp. 798-804
    • Scornik, O.A.1    Botbol, V.2
  • 14
    • 0017131813 scopus 로고
    • Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomer
    • Suda, H.; Aoyagi, T.; Takeuchi, T.; Umezawa, H. Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomer. Arch. Biochem. Biophys. 1976, 177 (1), 196-200.
    • (1976) Arch. Biochem. Biophys , vol.177 , Issue.1 , pp. 196-200
    • Suda, H.1    Aoyagi, T.2    Takeuchi, T.3    Umezawa, H.4
  • 15
    • 33750531864 scopus 로고    scopus 로고
    • Innovative lead discovery strategies for tropical diseases
    • Nwaka, S.; Hudson, A. Innovative lead discovery strategies for tropical diseases. Nat. Rev. Drug Discovery 2006, 5 (11), 941-55.
    • (2006) Nat. Rev. Drug Discovery , vol.5 , Issue.11 , pp. 941-955
    • Nwaka, S.1    Hudson, A.2
  • 16
    • 33749245660 scopus 로고    scopus 로고
    • Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity
    • Chen, X.; Chong, C. R.; Shi, L.; Yoshimoto, T.; Sullivan, D. J.; Jr.; Liu, J. O. Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity. Proc. Natl. Acad. Sci. U.S.A. 2006, 103 (39), 14548-53.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , Issue.39 , pp. 14548-14553
    • Chen, X.1    Chong, C.R.2    Shi, L.3    Yoshimoto, T.4    Sullivan Jr., D.J.5    Liu, J.O.6
  • 17
    • 0034775098 scopus 로고    scopus 로고
    • Analysis of antimalarial synergy between bestatin and endoprotease inhibitors using statistical response-surface modelling
    • Gavigan, C. S.; Machado, S. G.; Dalton, J. P.; Bell, A. Analysis of antimalarial synergy between bestatin and endoprotease inhibitors using statistical response-surface modelling. Antimicrob. Agents Chemother. 2001, 45 (11), 3175-81.
    • (2001) Antimicrob. Agents Chemother , vol.45 , Issue.11 , pp. 3175-3181
    • Gavigan, C.S.1    Machado, S.G.2    Dalton, J.P.3    Bell, A.4
  • 18
    • 33846563919 scopus 로고    scopus 로고
    • Synergistic interactions of the antiretroviral protease inhibitors saquinavir and ritonavir with chloroquine and mefloquine against Plasmodium falciparum in vitro
    • Skinner-Adams, T. S.; Andrews, K. T.; Melville, L.; McCarthy, J.; Gardiner, D. L. Synergistic interactions of the antiretroviral protease inhibitors saquinavir and ritonavir with chloroquine and mefloquine against Plasmodium falciparum in vitro. Antimicrob. Agents Chemother. 2007, 51 (2), 759-62.
    • (2007) Antimicrob. Agents Chemother , vol.51 , Issue.2 , pp. 759-762
    • Skinner-Adams, T.S.1    Andrews, K.T.2    Melville, L.3    McCarthy, J.4    Gardiner, D.L.5
  • 19
    • 0021055002 scopus 로고    scopus 로고
    • Sakakibara, T.; Ito, K.; Irie, Y.; Hagiwara, T.; Sakai, Y.; Hayashi, M1; Kishi, H.; Sakamoto, M.; Suzuki, M.; Irie, Y.; et al. Toxicological, studies on bestatin. I. Acute toxicity test in mice, rats and dogs. Jpn. J. Antibiot. 1983, 36 (11), 2971-84.
    • Sakakibara, T.; Ito, K.; Irie, Y.; Hagiwara, T.; Sakai, Y.; Hayashi, M1; Kishi, H.; Sakamoto, M.; Suzuki, M.; Irie, Y.; et al. Toxicological, studies on bestatin. I. Acute toxicity test in mice, rats and dogs. Jpn. J. Antibiot. 1983, 36 (11), 2971-84.
  • 20
    • 0035041649 scopus 로고    scopus 로고
    • Bestatin as an experimental tool in mammals
    • Scornik, O. A.; Botbol, V. Bestatin as an experimental tool in mammals. Curr. Drug Metab. 2001, 2 (1), 67-85.
    • (2001) Curr. Drug Metab , vol.2 , Issue.1 , pp. 67-85
    • Scornik, O.A.1    Botbol, V.2
  • 21
    • 0038364080 scopus 로고    scopus 로고
    • Randomized double-blind placebo-controlled trial of bestatin in patients with resected stage I squamous-cell lung carcinoma
    • Ichinose, Y.; Genka, K.; Koike, T.; Kato, H.; Watanabe, Y.; Mori, T.; Iioka, S.; Sakuma, A.; Ohta, M., Randomized double-blind placebo-controlled trial of bestatin in patients with resected stage I squamous-cell lung carcinoma. J. Natl. Cancer Inst. 2003, 95 (8), 605-10.
    • (2003) J. Natl. Cancer Inst , vol.95 , Issue.8 , pp. 605-610
    • Ichinose, Y.1    Genka, K.2    Koike, T.3    Kato, H.4    Watanabe, Y.5    Mori, T.6    Iioka, S.7    Sakuma, A.8    Ohta, M.9
  • 22
    • 2442449149 scopus 로고    scopus 로고
    • Synthesis and activity of phosphinic tripeptide inhibitors of cathepsin C
    • Mucha, A.; Pawel, M.; Hurek, J.; Kafarski, P. Synthesis and activity of phosphinic tripeptide inhibitors of cathepsin C. Bioorg. Med. Chem. Lett. 2004, 14 (12), 3113-6.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , Issue.12 , pp. 3113-3116
    • Mucha, A.1    Pawel, M.2    Hurek, J.3    Kafarski, P.4
  • 23
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. The determination of enzyme inhibitor constants. Biochem. J. 1953, 55 (1), 170-1.
    • (1953) Biochem. J , vol.55 , Issue.1 , pp. 170-171
    • Dixon, M.1
  • 24
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F.; Walsh, C. T. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 1988, 61, 201-301.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 25
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A.; Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234 (3), 779-815.
    • (1993) J. Mol. Biol , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 26
    • 33750124980 scopus 로고    scopus 로고
    • Extra precision glide: Docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes
    • Friesner, R. A.; Murphy, R. B.; Repasky, M. P.; Frye, L. L.; Greenwood, J. R.; Halgren, T. A.; Sanschagrin, P. C.; Mainz, D. T. Extra precision glide: Docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes. J. Med. Chem. 2006, 49 (21), 6177-96.
    • (2006) J. Med. Chem , vol.49 , Issue.21 , pp. 6177-6196
    • Friesner, R.A.1    Murphy, R.B.2    Repasky, M.P.3    Frye, L.L.4    Greenwood, J.R.5    Halgren, T.A.6    Sanschagrin, P.C.7    Mainz, D.T.8
  • 27
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W.; Jensen, J. B. Human malaria parasites in continuous culture. Science 1976, 193 (4254), 673-5.
    • (1976) Science , vol.193 , Issue.4254 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 28
    • 0021029671 scopus 로고
    • An in vitro assay system for the identification of potential antimalarial drugs
    • Geary, T. G.; Divo, A. A.; Jensen, J. B. An in vitro assay system for the identification of potential antimalarial drugs. J. Parasitol. 1983, 69 (3), 577-83.
    • (1983) J. Parasitol , vol.69 , Issue.3 , pp. 577-583
    • Geary, T.G.1    Divo, A.A.2    Jensen, J.B.3
  • 29
    • 0027753162 scopus 로고
    • A comparison of three methods of estimating EC50 in studies of drug resistance of malaria parasites
    • Huber, W.; Koella, J. C. A comparison of three methods of estimating EC50 in studies of drug resistance of malaria parasites. Acta Trop. 1993, 55 (4), 257-61.
    • (1993) Acta Trop , vol.55 , Issue.4 , pp. 257-261
    • Huber, W.1    Koella, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.