Metallo-aminopeptidase inhibitors

Biochimie

Volumn 92, Issue 11, 2010, Pages 1509-1529

  Mucha, Artur ^a   Drag, Marcin ^a   Dalton, John P ^b   Kafarski, Paweł ^a  

^a WROCLAW UNIVERSITY OF TECHNOLOGY   (Poland)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

Aminopeptidase; Cancer; Diseases; Drug design; Drugs; Enzymes; Inhibitor; Malaria; Non covalent ligand

Indexed keywords

2 THIOLBESTATIN; 4 HYDROXYBESTATIN; ALDEHYDE; AMINO ACID DERIVATIVE; AMINOPEPTIDASE; AMINOPEPTIDASE P; ANTIINFECTIVE AGENT; ANTIMALARIAL AGENT; ANTINEOPLASTIC AGENT; ANTINOCICEPTIVE AGENT; ANTIPARASITIC AGENT; BESTATIN; BESTATIN DERIVATIVE; BETULIC ACID; BORONIC ACID DERIVATIVE; CHR 2797; CURCUMIN; CYTOSOL AMINOPEPTIDASE; FUMAGILLIN; FUMAGILLOL CHLOROACETYLCARBAMATE; GALLIC ACID DERIVATIVE; HYDROXAMIC ACID DERIVATIVE; METALLO AMINOPEPTIDASE; METALLO AMINOPEPTIDASE INHIBITOR; MICROSOMAL AMINOPEPTIDASE; OVALICIN; SULFONAMIDE; TETRALIN DERIVATIVE; TOSEDOSTAT; TRIPEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

ACUTE GRANULOCYTIC LEUKEMIA; ANTIANGIOGENIC ACTIVITY; ANTINEOPLASTIC ACTIVITY; ANTINOCICEPTION; BACILLUS THURINGIENSIS; BACTERIUM; CATALYSIS; CELL CYCLE G2 PHASE; CELL CYCLE M PHASE; CLINICAL TRIAL; COLWELLIA PSYCHRERYTHRAEA; COMPETITIVE INHIBITION; DRUG DESIGN; DRUG POTENCY; DRUG SAFETY; DRUG SELECTIVITY; DRUG TARGETING; DRUG TOLERABILITY; EIMERIA TENELLA; ENZYME MECHANISM; ESCHERICHIA COLI; EXPERIMENTAL MOUSE; GEOBACILLUS THERMOLEOVORANS; HELICOBACTER PYLORI; HUMAN; IMMUNOMODULATION; LEGIONELLA PNEUMOPHILA; LISTONELLA ANGUILLARUM; MYCOBACTERIUM TUBERCULOSIS; MYELODYSPLASTIC SYNDROME; NONHUMAN; PHASE TRANSITION; PLASMODIUM CHABAUDI; PLASMODIUM FALCIPARUM; PYROCOCCUS FURIOSUS; REVIEW; STRUCTURE ACTIVITY RELATION;

AMINOPEPTIDASES; ANIMALS; BIOCATALYSIS; HUMANS; PROTEASE INHIBITORS;

EUKARYOTA; PROKARYOTA;

EID: 78149359487     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.04.026     Document Type: Review

References (201)

1. Hooper N.M., Lendeckel U. Aminopeptidases in Biology and Disease, Proteases in Biology and Disease 2004, vol. 2. Kluwer Academic/Plenum Publishers, New York.
2. Sanderink G.J., Artur Y., Siest G. Human aminopeptidases: a review of the literature. J. Clin. Chem. Clin. Biochem. 1988, 26:795-807.
3. Sanz Y. Aminopeptidases. Industrial Enzymes 2007, 243-260. Springer. J. Polaina, A.P. MacCabe (Eds.).
4. Jankiewicz U., Bielawski W. The properties and functions of bacterial aminopeptidases. Acta Microbiol. Pol. 2003, 52:217-231.
5. Rawlings N.D., Morton F.R., Kok C.Y., Kong J., Barrett A.J. MEROPS: the peptidase database. Nucleic Acids Res. 2008, 36:D320-D325.
6. Grembecka J., Kafarski P. Leucine aminopeptidase as a target for inhibitor design. Mini Rev. Med. Chem. 2001, 1:133-144.
7. York L.A., Goldberg A.L., Mo X.Y., Rock K.L. Proteolysis and class I major histocompatibility complex antigen presentation. Immunol. Rev. 1999, 172:49-66.
8. Towne C.F., York I.A., Neijssen J., Karow M.L., Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Neefjes J.J., Rock K.L. Leucine aminopeptidase is not essential for trimming peptides in the cytosol or generating epitopes for MHC class I antigen presentation. J. Immunol. 2005, 175:6605-6614.
9. Beninga J., Rock K.L., Goldberg A.L. Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 1998, 273:18734-18742.
10. Taylor A., Daims M., Lee J., Surgenor T. Identification and quantification of leucine aminopeptidase in aged normal and cataractous human lenses and ability of bovine lens LAP to cleave bovine crystallins. Curr. Eye Res. 1982, 2:47-56.
11. Kazeto H., Nomura S., Ito N., Ito T., Watanabe Y., Kajiyama H., Shibata K., Ino K., Tamakoshi K., Hattori A., Kikkawa F., Nagasaka T., Tsujimoto M., Mizutani S. Expression of adipocyte-derived leucine aminopeptidase in endometrial cancer. Association with tumor grade and CA-125. Tumour Biol. 2003, 24:203-208.
12. Pulido-Cejudo G., Conway B., Proulx P., Brown R., Izaguirre C.A. Bestatin-mediated inhibition of leucine aminopeptidase may hinder HIV infection. Antivir. Res. 1997, 36:167-177.
13. Mina-Osorio P. The moonlighting enzyme CD13: old and new functions to target. Trends Mol. Med. 2008, 14:361-371.
14. Potolicchio I., Carven G.J., Xu X., Stipp C., Riese R.J., Stern L.J., Santambrogio L. Proteomic analysis of microglia-derived exosomes: metabolic role of the aminopeptidase CD13 in neuropeptide catabolism. J. Immunol. 2005, 175:2237-2243.
15. Paul M., Poyan Mehr A., Kreutz R. Physiology of local renin-angiotensin systems. Physiol. Rev. 2006, 86:747-803.
16. Riemann D., Kehlen A., Langner J. CD13-not just a marker in leukemia typing. Immunol. Today 1999, 20:83-88.
17. Soderberg C., Giugni T.D., Zaia J.A., Larsson S., Wahlberg J.M., Moller E. CD13 (human aminopeptidase N) mediates human cytomegalovirus infection. J. Virol. 1993, 67:6576-6585.
18. Lassnig C., Sanchez C.M., Egerbacher M., Walter I., Majer S., Kolbe T., Pallares P., Enjuanes L., Muller M. Development of a transgenic mouse model susceptible to human coronavirus 229E. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:8275-8280.
19. Danziger R.S. Aminopeptidase N in arterial hypertension. Heart Fail. Rev. 2008, 13:293-298.
20. Lucius R., Sievers J., Mentlein R. Enkephalin metabolism by microglial aminopeptidase N (CD13). J. Neurochem. 1995, 64:1841-1847.
21. Rangel R., Sun Y., Guzman-Rojas L., Ozawa M.G., Sun J., Giordano R.J., Van Pelt C.S., Tinkey P.T., Behringer R.R., Sidman R.L., Arap W., Pasqualini R. Impaired angiogenesis in aminopeptidase N-null mice. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:4588-4593.
22. Mina-Osorio P., Winnicka B., O'Conor C., Grant C.L., Vogel L.K., Rodriguez-Pinto D., Holmes K.V., Ortega E., Shapiro L.H. CD13 is a novel mediator of monocytic/endothelial cell adhesion. J. Leukoc. Biol. 2008, 84:448-459.
23. Datta B. MAPs and POEP of the roads from prokaryotic to eukaryotic kingdoms. Biochimie 2000, 82:95-107.
24. Selvakumar P., Lakshmikuttyamma A., Dimmock J.R., Sharma R.K. Methionine aminopeptidase 2 and cancer. Biochim. Biophys. Acta 2006, 1765:148-154.
25. Priest R.C., Spaull J., Buckton J., Grimley R.L., Sims M., Binks M., Malhotra R. Immunomodulatory activity of a methionine aminopeptidase-2 inhibitor on B cell differentiation. Clin. Exp. Immunol. 2009, 155:514-522.
26. Tucker L.A., Zhang Q., Sheppard G.S., Lou P., Jiang F., McKeegan E., Lesniewski R., Davidsen S.K., Bell R.L., Wang J. Ectopic expression of methionine aminopeptidase-2 causes cell transformation and stimulates proliferation. Oncogene 2008, 27:3967-3976.
27. Leszczyniecka M., Bhatia U., Cueto M., Nirmala N.R., Towbin H., Vattay A., Wang B., Zabludoff S., Phillips P.E. MAP1D, a novel methionine aminopeptidase family member is overexpressed in colon cancer. Oncogene 2006, 25:3471-3478.
28. Datta B. Roles of P67/MetAP2 as a tumor suppressor. Biochim. Biophys. Acta 2009, 1796:281-292.
29. Dasgupta B., Yi Y., Hegedus B., Weber J.D., Gutmann D.H. Cerebrospinal fluid proteomic analysis reveals dysregulation of methionine aminopeptidase-2 expression in human and mouse neurofibromatosis 1-associated glioma. Cancer Res. 2005, 65:9843-9850.
30. Liu B.X., Du X.L., Zhou L.G., Hara K., Su W.J., Cao M.J. Purification and characterization of a leucine aminopeptidase from the skeletal muscle of common carp (Cyprinus carpio). Food Chem. 2008, 108:140-147.
31. Wu G.P., Cao M.J., Chen Y., Liu B.X., Su W.J. Leucine aminopeptidase from red sea bream (Pagrus major) skeletal muscle: purification, characterization, cellular location, and tissue distribution. J. Agric. Food Chem. 2008, 56:9653-9660.
32. Rhyu M.R., Nishimura T., Kato Y., Okitani A., Kato H. Purification and properties of aminopeptidase H from chicken skeletal muscle. Eur. J. Biochem. 1992, 208:53-59.
33. Bozic N., Ivanovic J., Nenadovic V., Bergstrom J., Larsson T., Vujcic Z. Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2008, 149:454-462.
34. Kaur R., Agrawal N., Bhatnagar R. Purification and characterization of aminopeptidase N from Spodoptera litura expressed in Sf21 insect cells. Protein Expr. Purif. 2007, 54:267-274.
35. Zhang S., Cheng H., Gao Y., Wang G., Liang G., Wu K. Mutation of an aminopeptidase N gene is associated with Helicoverpa armigera resistance to Bacillus thuringiensis Cry1Ac toxin. Insect Biochem. Mol. Biol. 2009, 39:421-429.
36. Chen J., Aimanova K.G., Pan S., Gill S.S. Identification and characterization of Aedes aegypti aminopeptidase N as a putative receptor of Bacillus thuringiensis Cry11A toxin. Insect Biochem. Mol. Biol. 2009, 39:688-696.
37. Isaac R.E., Bland N.D., Shirras A.D. Neuropeptidases and the metabolic inactivation of insect neuropeptides. Gen. Comp. Endocrinol. 2009, 162:8-17.
38. Graham S.C., Guss J.M. Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu. Arch. Biochem. Biophys. 2008, 469:200-208.
39. Zhang X., Chen S., Hu Z., Zhang L., Wang H. Expression and characterization of two functional methionine aminopeptidases from Mycobacterium tuberculosis H37Rv. Curr. Microbiol. 2009, 59:520-525.
40. Dong L., Cheng N., Wang M.W., Zhang J., Shu C., Zhu D.X. The leucyl aminopeptidase from Helicobacter pylori is an allosteric enzyme. Microbiology 2005, 151:2017-2023.
41. Bauvois C., Jacquamet L., Huston A.L., Borel F., Feller G., Ferrer J.L. Crystal structure of the cold-active aminopeptidase from Colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolase. J. Biol. Chem. 2008, 283:23315-23325.
42. Deejing S., Yoshimune K., Lumyong S., Moriguchi M. Purification and characterization of hyperthermotolerant leucine aminopeptidase from Geobacillus thermoleovorans 47b. J. Ind. Microbiol. Biotechnol. 2005, 32:269-276.
43. Yang H., Chen J., Yang G., Zhang X.H., Li Y. Mutational analysis of the zinc metalloprotease EmpA of Vibrio anguillarum. FEMS Microbiol. Lett. 2007, 267:56-63.
44. Story S.V., Shah C., Jenney F.E., Adams M.W. Characterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 2005, 187:2077-2083.
45. Stack C.M., Lowther J., Cunningham E., Donnelly S., Gardiner D.L., Trenholme K.R., Skinner-Adams T.S., Teuscher F., Grembecka J., Mucha A., Kafarski P., Lua L., Bell A., Dalton J.P. Characterization of the Plasmodium falciparum M17 leucyl aminopeptidase. A protease involved in amino acid regulation with potential for antimalarial drug development. J. Biol. Chem. 2007, 282:2069-2080.
46. Maric S., Donnelly S.M., Robinson M.W., Skinner-Adams T.S., Trenholme K.R., Gardiner D.L., Dalton J.P., Stack C.M., Lowther J. The M17 leucine aminopeptidase of the malaria parasite Plasmodium falciparum: importance of active site metal ions in the binding of substrates and inhibitors. Biochemistry 2009, 48:5435-5439.
47. Skinner-Adams T.S., Stack C.M., Trenholme K.R., Brown C.L., Grembecka J., Lowther J., Mucha A., Drag M., Kafarski P., McGowan S., Whisstock J.C., Gardiner D.L., Dalton J.P. Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials. Trends Biochem. Sci. 2010, 35:53-61.
48. Lauterbach S.B., Coetzer T.L. The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro. Malar. J. 2008, 7:161.
49. Teuscher F., Lowther J., Skinner-Adams T.S., Spielmann T., Dixon M.W., Stack C.M., Donnelly S., Mucha A., Kafarski P., Vassiliou S., Gardiner D.L., Dalton J.P., Trenholme K.R. The M18 aspartyl aminopeptidase of the human malaria parasite Plasmodium falciparum. J. Biol. Chem. 2007, 282:30817-30826.
50. Rossier O., Dao J., Cianciotto N.P. The type II secretion system of Legionella pneumophila elaborates two aminopeptidases, as well as a metalloprotease that contributes to differential infection among protozoan hosts. Appl. Environ. Microbiol. 2008, 74:753-761.
51. Fetterer R.H., Misk K.B., Barfield R.C. Partial purification and characterization of an aminopeptidase from Eimeria tenella. J. Parasitol. 2005, 91:1280-1286.
52. Jia H., Terkawi M.A., Aboge G.O., Goo Y.K., Luo Y., Li Y., Yamagishi J., Nishikawa Y., Igarashi I., Sugimoto C., Fujisaki K., Xuan X. Characterization of a leucine aminopeptidase of Babesia gibsoni. Parasitology 2009, 136:945-952.
53. Zhang H., Huang H., Cali A., Takvorian P.M., Feng X., Zhou G., Weiss L.M. Investigations into microsporidian methionine aminopeptidase type 2: a therapeutic target for microsporidiosis. Folia Parasitol. (Praha) 2005, 52:182-192.
54. McCarthy E., Stack C.N., Donnelly S.M., Doyle S., Mann V.H., Brindley P.J., Stewart M., Day T.A., Maule A.G., Dalton J.P. Leucine aminopeptidases of the human blood flukes Schistosoma mansoni and Schistosoma japonicum. Int. J. Parasitol. 2004, 34:703-714.
55. Rinaldi G., Morales M.E., Alrefaei Y.N., Cancela M., Castillo E., Dalton J.P., Tort J.F., Brindley P.J. RNA interference targeting leucine aminopeptidase blocks hatching of Schistosoma mansoni eggs. Mol. Biochem. Parasitol. 2009, 167:118-126.
56. Song S.M., Park J.H., Kim J., Kim S.I., Hong Y.C., Kong H.H., Chung D.I. Identification and characterization of Paragonimus westermani leucine aminopeptidase. Parasitol. Int. 2008, 57:334-341.
57. Acosta D., Cancela M., Piacenza L., Roche L., Carmona C., Tort J.F. Fasciola hepatica leucine aminopeptidase, a promising candidate for vaccination against ruminant fasciolosis. Mol. Biochem. Parasitol. 2008, 158:52-64.
58. Ercan A., Tay W.M., Grossman S.H., Ming L.J. Mechanistic role of each metal ion in Streptomyces dinuclear aminopeptidase: PEPTIDE hydrolysis and 7 × 10(10)-fold rate enhancement of phosphodiester hydrolysis. J. Inorg. Biochem. 2010, 104:19-29.
59. Cappiello M., Alterio V., Amodeo P., Del Corso A., Scaloni A., Pedone C., Moschini R., De Donatis G.M., De Simone G., Mura U. Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidase. Biochemistry 2006, 45:3226-3234.
60. Mitra S., Sheppard G., Wang J., Bennett B., Holz R.C. Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosus. J. Biol. Inorg. Chem. 2009, 14:573-585.
61. Chi M.C., Ong P.L., Hsu W.H., Chen Y.H., Huang H.B., Lin L.L. Role of the invariant Asn345 and Asn435 residues in a leucine aminopeptidase from Bacillus kaustophilus as evaluated by site-directed mutagenesis. Int. J. Biol. Macromol. 2008, 43:481-487.
62. Kapoor D., Singh B., Karthikeyan S., Guptasarma P. A functional comparison of the TET aminopeptidases of P. furiosus and B. subtilis with a protein-engineered variant recombining the former's structure with the latter's active site. Enzyme Microb. Technol. 2010, 46:1-8.
63. Hwang G.Y., Kuo L.Y., Tsai M.R., Yang S.L., Lin L.L. Histidines 345 and 378 of Bacillus stearothermophilus leucine aminopeptidase II are essential for the catalytic activity of the enzyme. Antonie Van Leeuwenhoek 2005, 87:355-359.
64. Mitra S., Job K.M., Meng L., Bennett B., Holz R.C. Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli. FEBS J. 2008, 275:6248-6259.
65. Watterson S.J., Mitra S., Swierczek S.I., Bennett B., Holz R.C. Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli. Biochemistry 2008, 47:11885-11893.
66. Bzymek K.P., Moulin A., Swierczek S.I., Ringe D., Petsko G.A., Bennett B., Holz R.C. Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase from Aeromonas proteolytica. Biochemistry 2005, 44:12030-12040.
67. Bzymek K.P., Holz R.C. The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica. J. Biol. Chem. 2004, 279:31018-31025.
68. Alvarado J.J., Nemkal A., Sauder J.M., Russell M., Akiyoshi D.E., Shi W., Almo S.C., Weiss L.M. Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470. Mol. Biochem. Parasitol. 2009, 168:158-167.
69. Michalska K., Brzezinski K., Jaskolski M. Crystal structure of isoaspartyl aminopeptidase in complex with l-aspartate. J. Biol. Chem. 2005, 280:28484-28491.
70. Fournie-Zaluski M.C., Poras H., Roques B.P., Nakajima Y., Ito K., Yoshimoto T. Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250. Acta Crystallogr. D Biol. Crystallogr. 2009, 65:814-822.
71. Ye Q.Z., Xie S.X., Ma Z.Q., Huang M., Hanzlik R.P. Structural basis of catalysis by monometalated methionine aminopeptidase. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:9470-9475.
72. Ataie N.J., Hoang Q.Q., Zahniser M.P., Tu Y., Milne A., Petsko G.A., Ringe D. Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus. Biochemistry 2008, 47:7673-7683.
73. Nocek B., Mulligan R., Bargassa M., Collart F., Joachimiak A. Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis. Proteins 2008, 70:273-279.
74. Douangamath A., Dale G.E., D'Arcy A., Almstetter M., Eckl R., Frutos-Hoener A., Henkel B., Illgen K., Nerdinger S., Schulz H., MacSweeney A., Thormann M., Treml A., Pierau S., Wadman S., Oefner C. Crystal structures of Staphylococcus aureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate. J. Med. Chem. 2004, 47:1325-1328.
75. McGowan S., Porter C.J., Lowther J., Stack C.M., Golding S.J., Skinner-Adams T.S., Trenholme K.R., Teuscher F., Donnelly S.M., Grembecka J., Mucha A., Kafarski P., Degori R., Buckle A.M., Gardiner D.L., Whisstock J.C., Dalton J.P. Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:2537-2542.
76. McGowan S., Oellig C.A., Birru W.A., Caradoc-Davies T.T., Stack C.M., Lowther J., Skinner-Adams T.S., Mucha A., Kafarski P., Grembecka J., Trenholme K.R., Buckle A.M., Gardiner D.L., Dalton J.P., Whisstock J.C. Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:2449-2454.
77. Chen S.L., Marino T., Fang W.H., Russo N., Himo F. Peptide hydrolysis by the binuclear zinc enzyme aminopeptidase from Aeromonas proteolytica: a density functional theory study. J. Phys. Chem. B 2008, 112:2494-2500.
78. Schurer G., Horn A.H.C., Gedeck P., Clark T. The reaction mechanism of bovine lens leucine aminopeptidase. J. Phys. Chem. B 2002, 106:8815-8830.
79. Jaime E., Kluge S., Weston J. On the origin of the broad-band selectivity of bovine-lens-leucine-aminopeptidase. Arkivoc 2007, 77-95.
80. Erhardt S., Weston J. Development of a working model of the active site in bovine lens leucine aminopeptidase: a density functional investigation. Chembiochem 2002, 3:101-104.
81. Bienvenue D.L., Gilner D., Holz R.C. Hydrolysis of thionopeptides by the aminopeptidase from Aeromonas proteolytica: insight into substrate binding. Biochemistry 2002, 41:3712-3719.
82. Kodanko J.J., Xu D., Song D.T., Lippard S.J. Iron substitution for sodium in a carboxylate-bridged, heterodinuclear sodium-iron complex. J. Am. Chem. Soc. 2005, 127:16004-16005.
83. Zhang X., Xu W. Aminopeptidase N (APN/CD13) as a target for anti-cancer agent design. Curr. Med. Chem. 2008, 15:2850-2865.
84. Lowther W.T., Matthews B.W. Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem. Rev. 2002, 102:4581-4608.
85. Bauvois B., Dauzonne D. Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects. Med. Res. Rev. 2006, 26:88-130.
86. Luan Y., Xu W. The structure and main functions of aminopeptidase N. Curr. Med. Chem. 2007, 14:639-647.
87. Giannousis P.P., Bartlett P.A. Phosphorus amino acid analogues as inhibitors of leucine aminopeptidase. J. Med. Chem. 1987, 30:1603-1609.
88. Lejczak B., Kafarski P. Biological activity of aminophosphonic acids and their short peptides. Top. Heterocycl. Chem. 2009, 20:31-63.
89. Lejczak B., De Choszczak M.P., Kafarski P. Inhibition of aminopeptidases by phosphonic acid and phosphinic acid analogues of aspartic and glutamic acids. J. Enzyme Inhib. 1993, 7:97-103.
90. Lejczak B., Kafarski P., Zygmunt J. Inhibition of aminopeptidases by aminophosphonates. Biochemistry 1989, 28:3549-3555.
91. Drag M., Grembecka J., Pawelczak M., Kafarski P. alpha-Aminoalkylphosphonates as a tool in experimental optimisation of P1 side chain shape of potential inhibitors in S1 pocket of leucine- and neutral aminopeptidases. Eur. J. Med. Chem. 2005, 40:764-771.
92. Drag M., Pawelczak M., Kafarski P. Stereoselective synthesis of 1-aminoalkanephosphonic acids with two chiral centers and their activity towards leucine aminopeptidase. Chirality 2003, 15:S104-S107.
93. Cunningham E., Drag M., Kafarski P., Bell A. Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitors. Antimicrob. Agents Chemother. 2008, 52:3221-3228.
94. Drag M., Bogyo M., Ellman J.A., Salvesen G.S. Aminopeptidase fingerprints. An integrated approach for identification of good substrates and optimal inhibitors. J. Biol. Chem. 2010, 285:3310-3318.
95. 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, 46:2641-2655.
96. Grembecka J., Sokalski W.A., Kafarski P. Computer-aided design and activity prediction of leucine aminopeptidase inhibitors. J. Comput. Aided Mol. Des. 2000, 14:531-544.
97. Grembecka J., Sokalski W.A., Kafarski P. Quantum chemical analysis of the interactions of transition state analogs with leucine aminopeptidase. Inter. J. Quant. Chem. 2001, 84:302-310.
98. Mucha A., Grembecka J., Cierpicki T., Kafarski P. Hydrolysis of the phosphonamidate bond in phosphono dipeptide analogues - the influence of the nature of the N-terminal functional group. Eur. J. Org. Chem. 2003, 4797-4803.
99. Mucha A., Laemmerhofer M., Lindner W., Pawelczak M., Kafarski P. Individual stereoisomers of phosphinic dipeptide inhibitor of leucine aminopeptidase. Bioorg. Med. Chem. Lett. 2008, 18:1550-1554.
100. Vassiliou S., Xeilari M., Yiotakis A., Grembecka J., Pawelczak M., Kafarski P., Mucha A. A synthetic method for diversification of the P1' substituent in phosphinic dipeptides as a tool for exploration of the specificity of the S1' binding pockets of leucine aminopeptidases. Bioorg. Med. Chem. 2007, 15:3187-3200.
101. Skinner-Adams T.S., Lowther J., Teuscher F., Stack C.M., Grembecka J., Mucha A., Kafarski P., Trenholme K.R., Dalton J.P., Gardiner D.L. Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds. J. Med. Chem. 2007, 50:6024-6031.
102. Chen H.X., Roques B.P., Fournie-Zaluski M.C. Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor. Bioorg. Med. Chem. Lett. 1999, 9:1511-1516.
103. Chen H.X., Noble F., Mothe A., Meudal H., Coric P., Danascimento S., Roques B.P., George P., Fournie-Zaluski M.C. Phosphinic derivatives as new dual enkephalin-degrading enzyme inhibitors: synthesis, biological properties, and antinociceptive activities. J. Med. Chem. 2000, 43:1398-1408.
104. Tholander F., Muroya A., Roques B.P., Fournie-Zaluski M.C., Thunnissen M.M.G.M., Haeggstrom J.Z. Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. 2008, 15:920-929.
105. Georgiadis D., Vazeux G., Llorens-Cortes C., Yiotakis A., Dive V. Potent and selective inhibition of zinc aminopeptidase A (EC 3.4.11.7, APA) by glutamyl aminophosphinic peptides: importance of glutamyl aminophosphinic residue in the P-1 position. Biochemistry 2000, 39:1152-1155.
106. Drag M., Grzywa R., Oleksyszyn J. Novel hydroxamic acid-related phosphinates: inhibition of neutral aminopeptidase N (APN). Bioorg. Med. Chem. Lett. 2007, 17:1516-1519.
107. Grzywa R., Oleksyszyn J. First synthesis of alpha-aminoalkyl-(N-substituted)thiocarbamoyl-phosphinates: inhibitors of aminopeptidase N (APN/CD13) with the new zinc-binding group. Bioorg. Med. Chem. Lett. 2008, 18:3734-3736.
108. Umezawa H., Aoyagi T., Suda H., Hamada M., Takeuchi T. Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes. J. Antibiot. (Tokyo) 1976, 29:97-99.
109. Scornik O.A., Botbol V. Bestatin as an experimental tool in mammals. Curr. Drug Metab. 2001, 2:67-85.
110. Burley S.K., David P.R., Lipscomb W.N. Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:6916-6920.
111. Orning L., Krivi G., Fitzpatrick F.A. Leukotriene A4 hydrolase. Inhibition by bestatin and intrinsic aminopeptidase activity establish its functional resemblance to metallohydrolase enzymes. J. Biol. Chem. 1991, 266:1375-1378.
112. Leyhausen G., Schuster D.K., Vaith P., Zahn R.K., Umezawa H., Falke D., Muller W.E. Identification and properties of the cell membrane bound leucine aminopeptidase interacting with the potential immunostimulant and chemotherapeutic agent bestatin. Biochem. Pharmacol. 1983, 32:1051-1057.
113. Rich D.H., Moon B.J., Harbeson S. Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes. J. Med. Chem. 1984, 27:417-422.
114. Suda H., Takita T., Aoyagi T., Umezawa H. The structure of bestatin. J. Antibiot. (Tokyo) 1976, 29:100-101.
115. Norman B.H., Morris M.L. A stereospecific synthesis of (-)-Bestatin from l-malic acid. Tetrahedron Lett. 1992, 33:6803-6806.
116. Wasserman H.H., Petersen A.K., Xia M.D. Application of acyl cyanophosphorane methodology to the synthesis of protease inhibitors: poststatin, eurystatin, phebestin, probestin and bestatin. Tetrahedron 2003, 59:6771-6784.
117. Bergmeier S.C., Stanchina D.M. Acylnitrene route to vicinal amino alcohols. Application to the synthesis of (-)-bestatin and analogues. J. Org. Chem. 1999, 64:2852-2859.
118. Nemoto H., Ma R.J., Suzuki I., Shibuya M. A new one-pot method for the synthesis of alpha-siloxyamides from aldehydes or ketones and its application to the synthesis of (-)-bestatin. Org. Lett. 2000, 2:4245-4247.
119. Righi G., D'Achille C., Pescatore G., Bonini C. New stereoselective synthesis of the peptidic aminopeptidase inhibitors bestatin, phebestin and probestin. Tetrahedron Lett. 2003, 44:6999-7002.
120. Feske B.D. Bestatin: three decades of synthetic strategies. Curr. Org. Chem. 2007, 11:483-496.
121. Luan Y.P., Mu J.J., Xu W.F. The review of the synthesis of bestatin, an effective inhibitor of aminopeptidase N. Mini Rev. Org. Chem. 2008, 5:134-140.
122. Evans J.F., Kargman S. Bestatin inhibits covalent coupling of [3H]LTA4 to human leukocyte LTA4 hydrolase. FEBS Lett. 1992, 297:139-142.
123. Gordon E.M., Godfrey J.D., Delaney N.G., Asaad M.M., Von Langen D., Cushman D.W. Design of novel inhibitors of aminopeptidases. Synthesis of peptide-derived diamino thiols and sulfur replacement analogues of bestatin. J. Med. Chem. 1988, 31:2199-2211.
124. Saino T., Seya K., Nishizawa R., Takita T., Aoyagi T., Umezawa H. Synthesis of p-hydroxyubenimex. J. Antibiot. (Tokyo) 1987, 40:1165-1169.
125. Ocain T.D., Rich D.H. Synthesis of sulfur-containing analogues of bestatin. Inhibition of aminopeptidases by alpha-thiolbestatin analogues. J. Med. Chem. 1988, 31:2193-2199.
126. Harbut M.B., Velmourougane G., Reiss G., Chandramohanadas R., Greenbaum D.C. Development of bestatin-based activity-based probes for metallo-aminopeptidases. Bioorg. Med. Chem. Lett. 2008, 18:5932-5936.
127. Nagai M., Kojima F., Naganawa H., Hamada M., Aoyagi T., Takeuchi T. Phebestin, a new inhibitor of aminopeptidase N, produced by Streptomyces sp. MJ716-m3. J. Antibiot. (Tokyo) 1997, 50:82-84.
128. Aoyagi T., Yoshida S., Nakamura Y., Shigihara Y., Hamada M., Takeuchi T. Probestin, a new inhibitor of aminopeptidase M, produced by Streptomyces azureus MH663-2F6. I. Taxonomy, production, isolation, physico-chemical properties and biological activities. J. Antibiot. (Tokyo) 1990, 43:143-148.
129. Matsas R., Stephenson S.L., Hryszko J., Kenny A.J., Turner A.J. The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N. Biochem. J. 1985, 231:445-449.
130. Coussens L.M., Fingleton B., Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002, 295:2387-2392.
131. Fingleton B. Matrix metalloproteinase inhibitors for cancer therapy: the current situation and future prospects. Expert Opin. Ther. Targets 2003, 7:385-397.
132. Chan W.W., Dennis P., Demmer W., Brand K. Inhibition of leucine aminopeptidase by amino acid hydroxamates. J. Biol. Chem. 1982, 257:7955-7957.
133. Fournie-Zaluski M.C., Coric P., Turcaud S., Bruetschy L., Lucas E., Noble F., Roques B.P. Potent and systemically active aminopeptidase N inhibitors designed from active-site investigation. J. Med. Chem. 1992, 35:1259-1266.
134. Lee J., Shim J.S., Jung S.A., Lee S.T., Kwon H.J. N-hydroxy-2-(naphthalene-2-ylsulfanyl)-acetamide, a novel hydroxamic acid-based inhibitor of aminopeptidase N and its anti-angiogenic activity. Bioorg. Med. Chem. Lett. 2005, 15:181-183.
135. Hu X., Zhu J., Srivathsan S., Pei D. Peptidyl hydroxamic acids as methionine aminopeptidase inhibitors. Bioorg. Med. Chem. Lett. 2004, 14:77-79.
136. Huang Q.Q., Huang M., Nan F.J., Ye Q.Z. Metalloform-selective inhibition: synthesis and structure-activity analysis of Mn(II)-form-selective inhibitors of Escherichia coli methionine aminopeptidase. Bioorg. Med. Chem. Lett. 2005, 15:5386-5391.
137. Flipo M., Florent I., Grellier P., Sergheraert C., Deprez-Poulain R. Design, synthesis and antimalarial activity of novel, quinoline-based, zinc metallo-aminopeptidase inhibitors. Bioorg. Med. Chem. Lett. 2003, 13:2659-2662.
138. Flipo M., Beghyn T., Leroux V., Florent I., Deprez B.P., Deprez-Poulain R.F. Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents. J. Med. Chem. 2007, 50:1322-1334.
139. L.A. Pearson, A.P. Ayscough, P. Huxley, A.H. Drummond, Cytostatic Agents, 2002 (US Patent 5452023).
140. Krige D., Needham L.A., Bawden L.J., Flores N., Farmer H., Miles L.E., Stone E., Callaghan J., Chandler S., Clark V.L., Kirwin-Jones P., Legris V., Owen J., Patel T., Wood S., Box G., Laber D., Odedra R., Wright A., Wood L.M., Eccles S.A., Bone E.A., Ayscough A., Drummond A.H. CHR-2797: an antiproliferative aminopeptidase inhibitor that leads to amino acid deprivation in human leukemic cells. Cancer Res. 2008, 68:6669-6679.
141. Reid A.H., Protheroe A., Attard G., Hayward N., Vidal L., Spicer J., Shaw H.M., Bone E.A., Carter J., Hooftman L., Harris A., De Bono J.S. A first-in-man phase I and pharmacokinetic study on CHR-2797 (Tosedostat), an inhibitor of M1 aminopeptidases, in patients with advanced solid tumors. Clin. Cancer Res. 2009, 15:4978-4985.
142. Owen R.T., Castaner R., Bolos J. Tosedostat. Aminopeptidase inhibitor, oncolytic. Drugs Fut. 2009, 115-118.
143. Ocain T.D., Rich D.H. l-Lysinethiol: a subnanomolar inhibitor of aminopeptidase B. Biochem. Biophys. Res. Commun. 1987, 145:1038-1042.
144. Chan W.W. l-Leucinthiol - a potent inhibitor of leucine aminopeptidase. Biochem. Biophys. Res. Commun. 1983, 116:297-302.
145. Chauvel E.N., Coric P., Llorens-Cortes C., Wilk S., Roques B.P., Fournie-Zaluski M.C. Investigation of the active site of aminopeptidase A using a series of new thiol-containing inhibitors. J. Med. Chem. 1994, 37:1339-1346.
146. Chauvel E.N., Llorens-Cortes C., Coric P., Wilk S., Roques B.P., Fournie-Zaluski M.C. Differential inhibition of aminopeptidase A and aminopeptidase N by new beta-amino thiols. J. Med. Chem. 1994, 37:2950-2957.
147. Fournie-Zaluski M.C., Coric P., Turcaud S., Lucas E., Noble F., Maldonado R., Roques B.P. "Mixed inhibitor-prodrug" as a new approach toward systemically active inhibitors of enkephalin-degrading enzymes. J. Med. Chem. 1992, 35:2473-2481.
148. Wilk S., Thurston L.S. Inhibition of angiotensin III formation by thiol derivatives of acidic amino acids. Neuropeptides 1990, 16:163-168.
149. Reaux A., de Mota N., Zini S., Cadel S., Fournie-Zaluski M.C., Roques B.P., Corvol P., Llorens-Cortes C. PC18, a specific aminopeptidase N inhibitor, induces vasopressin release by increasing the half-life of brain angiotensin III. Neuroendocrinology 1999, 69:370-376.
150. David C., Bischoff L., Meudal H., Mothe A., De Mota N., DaNascimento S., Llorens-Cortes C., Fournie-Zaluski M.C., Roques B.P. Investigation of subsite preferences in aminopeptidase A (EC 3.4.11.7) led to the design of the first highly potent and selective inhibitors of this enzyme. J. Med. Chem. 1999, 42:5197-5211.
151. Inguimbert N., Coric P., Dhotel H., Bonnard E., Llorens-Cortes C., Mota N., Fournie-Zaluski M.C., Roques B.P. Synthesis and in vitro activities of new non-peptidic APA inhibitors. J. Pept. Res. 2005, 65:175-188.
152. Zini S., Fournie-Zaluski M.C., Chauvel E., Roques B.P., Corvol P., Llorens-Cortes C. Identification of metabolic pathways of brain angiotensin II and III using specific aminopeptidase inhibitors: predominant role of angiotensin III in the control of vasopressin release. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:11968-11973.
153. Reaux A., Fournie-Zaluski M.C., David C., Zini S., Roques B.P., Corvol P., Llorens-Cortes C. Aminopeptidase A inhibitors as potential central antihypertensive agents. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:13415-13420.
154. Fournie-Zaluski M.C., Fassot C., Valentin B., Djordjijevic D., Reaux-Le Goazigo A., Corvol P., Roques B.P., Llorens-Cortes C. Brain renin-angiotensin system blockade by systemically active aminopeptidase A inhibitors: a potential treatment of salt-dependent hypertension. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:7775-7780.
155. Bodineau L., Frugiere A., Marc Y., Inguimbert N., Fassot C., Balavoine F., Roques B.P., Llorens-Cortes C. Orally active aminopeptidase A inhibitors reduce blood pressure: a new strategy for treating hypertension. Hypertension 2008, 51:1318-1325.
156. Griffith E.C., Su Z., Turk B.E., Chen S., Chang Y.H., Wu Z., Biemann K., Liu J.O. Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin. Chem. Biol. 1997, 4:461-471.
157. Sin N., Meng L., Wang M.Q., Wen J.J., Bornmann W.G., Crews C.M. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:6099-6103.
158. Lowther W.T., McMillen D.A., Orville A.M., Matthews B.W. The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:12153-12157.
159. Liu S., Widom J., Kemp C.W., Crews C.M., Clardy J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science 1998, 282:1324-1327.
160. Turk B.E., Su Z., Liu J.O. Synthetic analogues of TNP-470 and ovalicin reveal a common molecular basis for inhibition of angiogenesis and immunosuppression. Bioorg. Med. Chem. 1998, 6:1163-1169.
161. Ye Q.Z., Xie S.X., Huang M., Huang W.J., Lu J.P., Ma Z.Q. Metalloform-selective inhibitors of Escherichia coli methionine aminopeptidase and X-ray structure of a Mn(II)-form enzyme complexed with an inhibitor. J. Am. Chem. Soc. 2004, 126:13940-13941.
162. Huang M., Xie S.X., Ma Z.Q., Huang Q.Q., Nan F.J., Ye Q.Z. Inhibition of monometalated methionine aminopeptidase: inhibitor discovery and crystallographic analysis. J. Med. Chem. 2007, 50:5735-5742.
163. Zhou Y., Guo X.C., Yi T., Yoshimoto T., Pei D. Two continuous spectrophotometric assays for methionine aminopeptidase. Anal. Biochem. 2000, 280:159-165.
164. Hu X., Addlagatta A., Matthews B.W., Liu J.O. Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases. Angew. Chem. Int. Ed. Engl. 2006, 45:3772-3775.
165. Schiffmann R., Heine A., Klebe G., Klein C.D. Metal ions as cofactors for the binding of inhibitors to methionine aminopeptidase: a critical view of the relevance of in vitro metalloenzyme assays. Angew. Chem. Int. Ed. Engl. 2005, 44:3620-3623.
166. Schiffmann R., Neugebauer A., Klein C.D. Metal-mediated inhibition of Escherichia coli methionine aminopeptidase: structure-activity relationships and development of a novel scoring function for metal-ligand interactions. J. Med. Chem. 2006, 49:511-522.
167. J.P. Marino Jr., D.F. Thompson, D.F. Veber, Substituted 1,2,4-Triazole Methionine Aminopeptidase Type 2 Inhibitors, their Preparation, and their Therapeutic Use, 2002 (Patent WO 2002078696).
168. J.P. Marino Jr., S.K. Thompson, D.F. Veber, Substituted Triazole Methionine Aminopeptidase Type 2 Inhibitors, their Preparation, and their Therapeutic Use, 2002 (Patent WO 2002078697).
169. Marino J.P., Fisher P.W., Hofmann G.A., Kirkpatrick R.B., Janson C.A., Johnson R.K., Ma C., Mattern M., Meek T.D., Ryan M.D., Schulz C., Smith W.W., Tew D.G., Tomazek T.A., Veber D.F., Xiong W.C., Yamamoto Y., Yamashita K., Yang G., Thompson S.K. Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore. J. Med. Chem. 2007, 50:3777-3785.
170. Kallander L.S., Lu Q., Chen W., Tomaszek T., Yang G., Tew D., Meek T.D., Hofmann G.A., Schulz-Pritchard C.K., Smith W.W., Janson C.A., Ryan M.D., Zhang G.F., Johanson K.O., Kirkpatrick R.B., Ho T.F., Fisher P.W., Mattern M.R., Johnson R.K., Hansbury M.J., Winkler J.D., Ward K.W., Veber D.F., Thompson S.K. 4-Aryl-1,2,3-triazole: a novel template for a reversible methionine aminopeptidase 2 inhibitor, optimized to inhibit angiogenesis in vivo. J. Med. Chem. 2005, 48:5644-5647.
171. Oefner C., Douangamath A., D'Arcy A., Hafeli S., Mareque D., Mac Sweeney A., Padilla J., Pierau S., Schulz H., Thormann M., Wadman S., Dale G.E. The 1.15A crystal structure of the Staphylococcus aureus methionyl-aminopeptidase and complexes with triazole based inhibitors. J. Mol. Biol. 2003, 332:13-21.
172. Wang J., Sheppard G.S., Lou P., Kawai M., Park C., Egan D.A., Schneider A., Bouska J., Lesniewski R., Henkin J. Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese. Biochemistry 2003, 42:5035-5042.
173. Garrabrant T., Tuman R.W., Ludovici D., Tominovich R., Simoneaux R.L., Galemmo R.A., Johnson D.L. Small molecule inhibitors of methionine aminopeptidase type 2 (MetAP-2). Angiogenesis 2004, 7:91-96.
174. Luo Q.L., Li J.Y., Liu Z.Y., Chen L.L., Li J., Qian Z., Shen Q., Li Y., Lushington G.H., Ye Q.Z., Nan F.J. Discovery and structural modification of inhibitors of methionine aminopeptidases from Escherichia coli and Saccharomyces cerevisiae. J. Med. Chem. 2003, 46:2631-2640.
175. Luo Q.L., Li J.Y., Chen L.L., Li J., Ye Q.Z., Nan F.J. Inhibitors of type I MetAPs containing pyridine-2-carboxylic acid thiazol-2-ylamide. Part 2: SAR studies on the pyridine ring 3-substituent. Bioorg. Med. Chem. Lett. 2005, 15:639-644.
176. Cui Y.M., Huang Q.Q., Xu J., Chen L.L., Li J.Y., Ye Q.Z., Li J., Nan F.J. Identification of potent type I MetAP inhibitors by simple bioisosteric replacement. Part 1: synthesis and preliminary SAR studies of thiazole-4-carboxylic acid thiazol-2-ylamide derivatives. Bioorg. Med. Chem. Lett. 2005, 15:3732-3736.
177. Cui Y.M., Huang Q.Q., Xu J., Chen L.L., Li J.Y., Ye Q.Z., Li J., Nan F.J. Identification of potent type I MetAPs inhibitors by simple bioisosteric replacement. Part 2: SAR studies of 5-heteroalkyl substituted TCAT derivatives. Bioorg. Med. Chem. Lett. 2005, 15:4130-4135.
178. Hu X., Addlagatta A., Lu J., Matthews B.W., Liu J.O. Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:18148-18153.
179. Wang W.L., Chai S.C., Huang M., He H.Z., Hurley T.D., Ye Q.Z. Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activity. J. Med. Chem. 2008, 51:6110-6120.
180. Chen X., Chong C.R., Shi L., Yoshimoto T., Sullivan D.J., Liu J.O. Inhibitors of Plasmodium falciparum methionine aminopeptidase 1b possess antimalarial activity. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:14548-14553.
181. Baker J.O., Wilkes S.H., Bayliss M.E., Prescott J.M. Hydroxamates and aliphatic boronic acids: marker inhibitors for aminopeptidase. Biochemistry 1983, 22:2098-2103.
182. Baker J.O., Prescott J.M. A transition-state-analog inhibitor influences zinc-binding by Aeromonas aminopeptidase. Biochem. Biophys. Res. Commun. 1985, 130:1154-1160.
183. Shenvi A.B. alpha-Aminoboronic acid derivatives: effective inhibitors of aminopeptidases. Biochemistry 1986, 25:1286-1291.
184. Andersson L., Isley T.C., Wolfenden R. alpha-Aminoaldehydes: transition state analogue inhibitors of leucine aminopeptidase. Biochemistry 1982, 21:4177-4180.
185. Tarnus C., Remy J.M., d'Orchymont H. 3-Amino-2-hydroxy-propionaldehyde and 3-amino-1-hydroxy-propan-2-one derivatives: new classes of aminopeptidase inhibitors. Bioorg. Med. Chem. 1996, 4:1287-1297.
186. Kawai M., BaMaung N.Y., Fidanze S.D., Erickson S.A., Tedrow J.S., Sanders W.J., Vasudevan A., Park C., Hutchins C., Comess K.M., Kalvin D., Wang J., Zhang Q., Lou P., Tucker-Garcia L., Bouska J., Bell R.L., Lesniewski R., Henkin J., Sheppard G.S. Development of sulfonamide compounds as potent methionine aminopeptidase type II inhibitors with antiproliferative properties. Bioorg. Med. Chem. Lett. 2006, 16:3574-3577.
187. Sheppard G.S., Wang J., Kawai M., Fidanze S.D., BaMaung N.Y., Erickson S.A., Barnes D.M., Tedrow J.S., Kolaczkowski L., Vasudevan A., Park D.C., Wang G.T., Sanders W.J., Mantei R.A., Palazzo F., Tucker-Garcia L., Lou P., Zhang Q., Park C.H., Kim K.H., Petros A., Olejniczak E., Nettesheim D., Hajduk P., Henkin J., Lesniewski R., Davidsen S.K., Bell R.L. Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding. J. Med. Chem. 2006, 49:3832-3849.
188. Wang G.T., Mantei R.A., Kawai M., Tedrow J.S., Barnes D.M., Wang J., Zhang Q., Lou P., Garcia L.A., Bouska J., Yates M., Park C., Judge R.A., Lesniewski R., Sheppard G.S., Bell R.L. Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids. Bioorg. Med. Chem. Lett. 2007, 17:2817-2822.
189. Wang J., Tucker L.A., Stavropoulos J., Zhang Q., Wang Y.C., Bukofzer G., Niquette A., Meulbroek J.A., Barnes D.M., Shen J., Bouska J., Donawho C., Sheppard G.S., Bell R.L. Correlation of tumor growth suppression and methionine aminopetidase-2 activity blockade using an orally active inhibitor. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:1838-1843.
190. Huang M., Xie S.X., Ma Z.Q., Hanzlik R.P., Ye Q.Z. Metal mediated inhibition of methionine aminopeptidase by quinolinyl sulfonamides. Biochem. Biophys. Res. Commun. 2006, 339:506-513.
191. Schalk C., d'Orchymont H., Jauch M.F., Tarnus C. 3-Amino-2-tetralone derivatives: novel potent and selective inhibitors of aminopeptidase-M (EC 3.4.11.2). Arch. Biochem. Biophys. 1994, 311:42-46.
192. Albrecht S., Defoin A., Salomon E., Tarnus C., Wetterholm A., Haeggstrom J.Z. Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors. Bioorg. Med. Chem. 2006, 14:7241-7257.
193. Wang J.L., Xu W.F. The preparation of novel 1-iso-glutamine derivatives as potential antitumor agents. J. Chem. Res. Synop. 2003, 12:789.
194. W.F. Xu, Design, Synthesis and Antitumor Research of Peptidomimetic MMPIS, 226th ACS National Meeting, 2003, p. 7.
195. Li Q., Fang H., Xu W. Novel 3-galloylamido-N'-substituted-2,6-piperidinedione-N-acetamide peptidomimetics as metalloproteinase inhibitors. Bioorg. Med. Chem. Lett. 2007, 17:2935-2938.
196. Drag M., Surowiak P., Drag-Zalesinska M., Dietel M., Lage H., Oleksyszyn J. Comparison of the cytotoxic effects of birch bark extract, betulin and betulinic acid towards human gastric carcinoma and pancreatic carcinoma drug-sensitive and drug-resistant cell lines. Molecules 2009, 14:1639-1651.
197. Fulda S., Scaffidi C., Susin S.A., Krammer P.H., Kroemer G., Peter M.E., Debatin K.M. Activation of mitochondria and release of mitochondrial apoptogenic factors by betulinic acid. J. Biol. Chem. 1998, 273:33942-33948.
198. Melzig M.F., Bormann H. Betulinic acid inhibits aminopeptidase N activity. Planta Med. 1998, 64:655-657.
199. Thangapazham R.L., Sharma A., Maheshwari R.K. Multiple molecular targets in cancer chemoprevention by curcumin. AAPS J. 2006, 8:E443-E449.
200. Kuttan G., Kumar K.B., Guruvayoorappan C., Kuttan R. Antitumor, anti-invasion, and antimetastatic effects of curcumin. Adv. Exp. Med. Biol. 2007, 595:173-184.
201. Shim J.S., Kim J.H., Cho H.Y., Yum Y.N., Kim S.H., Park H.J., Shim B.S., Choi S.H., Kwon H.J. Irreversible inhibition of CD13/aminopeptidase N by the antiangiogenic agent curcumin. Chem. Biol. 2003, 10:695-704.