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Volumn 73, Issue 1, 2009, Pages 75-82

Aromatic organic compounds as scaffolds for metallocarboxypeptidase inhibitor design

Author keywords

Aromatic organic derivative; Enzyme inhibition; Human carboxypeptidase B; In silico screening; Metallocarboxypeptidases; Molecular docking

Indexed keywords

2 [5 [(NAPHTHALEN 2 YLOXY)METHYL] 1,3,4 OXADIAZOL 2 YLTHIO] 1 (4 TOLYL)ETHANONE; AROMATIC COMPOUND; CARBOXYPEPTIDASE B; LIGAND; METALLOCARBOXYPEPTIDASE INHIBITOR; NAPHTHALENE DERIVATIVE; PROTEINASE; QUINAZOLINE DERIVATIVE; QUINOLINE DERIVATIVE; UNCLASSIFIED DRUG; ZINC ION;

EID: 58149084494     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2008.00752.x     Document Type: Article
Times cited : (4)

References (40)
  • 1
    • 37049247190 scopus 로고
    • Action of carboxypeptidase toward peptides containing unnatural aromatic amino acids
    • Dunn F.W., Dittmer K. (1950) Action of carboxypeptidase toward peptides containing unnatural aromatic amino acids. Science 111 : 173 175.
    • (1950) Science , vol.111 , pp. 173-175
    • Dunn, F.W.1    Dittmer, K.2
  • 2
    • 0037075108 scopus 로고    scopus 로고
    • Cysteine derivatives as inhibitors for carboxypeptidase A: Synthesis and structure-activity relationships
    • Park J.D., Kim D.H. (2002) Cysteine derivatives as inhibitors for carboxypeptidase A: synthesis and structure-activity relationships. J Med Chem 45 : 911 918.
    • (2002) J Med Chem , vol.45 , pp. 911-918
    • Park, J.D.1    Kim, D.H.2
  • 3
    • 0024519490 scopus 로고
    • An angiotensin converting enzyme inhibitor is a tight-binding slow substrate of carboxypeptidase a
    • Martin M.T., Holmquist B., Riordan J.F. (1989) An angiotensin converting enzyme inhibitor is a tight-binding slow substrate of carboxypeptidase A. J Inorg Biochem 36 : 39 50.
    • (1989) J Inorg Biochem , vol.36 , pp. 39-50
    • Martin, M.T.1    Holmquist, B.2    Riordan, J.F.3
  • 4
    • 0030927294 scopus 로고    scopus 로고
    • Inhibition of carboxypeptidase a by n-(4-t-butylbenzoyl)-2-hydroxy-1- naphthaldehyde hydrazone
    • Lanthier C.M., Parniak M.A., Dmitrenko G.I. (1997) Inhibition of carboxypeptidase A by n-(4-t-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone. Bioorg Med Chem Lett 7 : 1557 1562.
    • (1997) Bioorg Med Chem Lett , vol.7 , pp. 1557-1562
    • Lanthier, C.M.1    Parniak, M.A.2    Dmitrenko, G.I.3
  • 5
    • 0015424260 scopus 로고
    • Fluorescende determination of carboxypeptidase a activity based on electronic energy transfer
    • Latt S.A., Auld D.S., Vallee B.L. (1972) Fluorescende determination of carboxypeptidase A activity based on electronic energy transfer. Anal Biochem 50 : 56 62.
    • (1972) Anal Biochem , vol.50 , pp. 56-62
    • Latt, S.A.1    Auld, D.S.2    Vallee, B.L.3
  • 6
    • 0029007061 scopus 로고
    • Highly sensitive high-performance liquid chromatography-fluorimetric assay method for carboxypeptidase H activity
    • Yajima R., Chikuma T., Kato T. (1995) Highly sensitive high-performance liquid chromatography-fluorimetric assay method for carboxypeptidase H activity. J Chromatogr B Biomed Appl 667 : 333 338.
    • (1995) J Chromatogr B Biomed Appl , vol.667 , pp. 333-338
    • Yajima, R.1    Chikuma, T.2    Kato, T.3
  • 7
    • 50549209602 scopus 로고
    • Inhibition of several enzymes by folic acid, aminopterin and amethopterin
    • Vogel W.H., Snyder R., Schulman M.P. (1964) Inhibition of several enzymes by folic acid, aminopterin and amethopterin. Biochim Biophys Acta 85 : 164 166.
    • (1964) Biochim Biophys Acta , vol.85 , pp. 164-166
    • Vogel, W.H.1    Snyder, R.2    Schulman, M.P.3
  • 8
    • 21144456472 scopus 로고
    • Effects of aromatic and nonaromatic model compounds and drugs on enzymic activities
    • Vogel W.H., Snyder R., Schulman M.P. (1964) Effects of aromatic and nonaromatic model compounds and drugs on enzymic activities. J Pharmacol Exp Ther 146 : 66 73.
    • (1964) J Pharmacol Exp Ther , vol.146 , pp. 66-73
    • Vogel, W.H.1    Snyder, R.2    Schulman, M.P.3
  • 9
    • 20444460605 scopus 로고    scopus 로고
    • Metallocarboxypeptidases
    • In: Messerschmidt, A., Bode, W., Cygler, M., editors. Chichester: John Wiley & Sons, Ltd. p.
    • Vendrell J., Aviles F.X., Fricker L.D. (2004) Metallocarboxypeptidases. In : Messerschmidt A., Bode W., Cygler M., editors. Metallocarboxypeptidases. Chichester : John Wiley & Sons, Ltd p. 176 189.
    • (2004) Metallocarboxypeptidases. , pp. 176-189
    • Vendrell, J.1    Aviles, F.X.2    Fricker, L.D.3
  • 11
    • 33846957741 scopus 로고    scopus 로고
    • Serum carboxypeptidase a activity as a biomarker for early-stage pancreatic carcinoma
    • Matsugi S., Hamada T., Shioi N., Tanaka T., Kumada T., Satomura S. (2007) Serum carboxypeptidase A activity as a biomarker for early-stage pancreatic carcinoma. Clin Chim Acta 378 : 147 153.
    • (2007) Clin Chim Acta , vol.378 , pp. 147-153
    • Matsugi, S.1    Hamada, T.2    Shioi, N.3    Tanaka, T.4    Kumada, T.5    Satomura, S.6
  • 12
    • 37849187428 scopus 로고    scopus 로고
    • Evaluation of pro-carboxypeptidase a and carboxypeptidase a as serologic markers for adenocarcinoma of the pancreas
    • Shamamian P., Goldberg J.D., Ye X.Y., Stewart J.D., White P.J., Gilvarg C. (2006) Evaluation of pro-carboxypeptidase A and carboxypeptidase A as serologic markers for adenocarcinoma of the pancreas. HPB (Oxford) 8 : 451 457.
    • (2006) HPB (Oxford) , vol.8 , pp. 451-457
    • Shamamian, P.1    Goldberg, J.D.2    Ye, X.Y.3    Stewart, J.D.4    White, P.J.5    Gilvarg, C.6
  • 13
    • 34247891640 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and its relationship to fibrinolysis and inflammation during the acute and convalescent phase of ischemic stroke
    • Rooth E., Wallen H., Antovic A., von Arbin M., Kaponides G., Wahlgren N., Blomback M., Antovic J. (2007) Thrombin activatable fibrinolysis inhibitor and its relationship to fibrinolysis and inflammation during the acute and convalescent phase of ischemic stroke. Blood Coagul Fibrinolysis 18 : 365 370.
    • (2007) Blood Coagul Fibrinolysis , vol.18 , pp. 365-370
    • Rooth, E.1    Wallen, H.2    Antovic, A.3    Von Arbin, M.4    Kaponides, G.5    Wahlgren, N.6    Blomback, M.7    Antovic, J.8
  • 14
    • 34147159934 scopus 로고    scopus 로고
    • A role for procarboxypepidase U (TAFI) in thrombosis
    • Willemse J.L., Hendriks D.F. (2007) A role for procarboxypepidase U (TAFI) in thrombosis. Front Biosci 12 : 1973 1987.
    • (2007) Front Biosci , vol.12 , pp. 1973-1987
    • Willemse, J.L.1    Hendriks, D.F.2
  • 15
    • 33846153546 scopus 로고    scopus 로고
    • Metallocarboxypeptidases: Emerging drug targets in biomedicine
    • Arolas J.L., Vendrell J., Aviles F.X., Fricker L.D. (2007) Metallocarboxypeptidases: emerging drug targets in biomedicine. Curr Pharm Des 13 : 349 366.
    • (2007) Curr Pharm des , vol.13 , pp. 349-366
    • Arolas, J.L.1    Vendrell, J.2    Aviles, F.X.3    Fricker, L.D.4
  • 16
    • 35548965455 scopus 로고    scopus 로고
    • Opportunities for structure-based design of protease-directed drugs
    • Mittl P.R., Grutter M.G. (2006) Opportunities for structure-based design of protease-directed drugs. Curr Opin Struct Biol 16 : 769 775.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 769-775
    • Mittl, P.R.1    Grutter, M.G.2
  • 17
    • 10744228937 scopus 로고    scopus 로고
    • Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics
    • Barrow J.C., Nantermet P.G., Stauffer S.R., Ngo P.L., Steinbeiser M.A., Mao S.S., Carroll S.S. et al. (2003) Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics. J Med Chem 46 : 5294 5297.
    • (2003) J Med Chem , vol.46 , pp. 5294-5297
    • Barrow, J.C.1    Nantermet, P.G.2    Stauffer, S.R.3    Ngo, P.L.4    Steinbeiser, M.A.5    Mao, S.S.6    Carroll, S.S.7
  • 19
    • 11144356646 scopus 로고    scopus 로고
    • Enhancement of fibrinolysis by EF6265 [(S)-7-amino-2-[[[(R)-2-methyl-1- (3-phenylpropanoylamino)propyl]hydroxypho sphinoyl] methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B
    • Suzuki K., Muto Y., Fushihara K., Kanemoto K., Iida H., Sato E., Kikuchi C., Matsushima T., Kato E., Nomoto M., Yoshioka S., Ishii H. (2004) Enhancement of fibrinolysis by EF6265 [(S)-7-amino-2-[[[(R)-2-methyl-1-(3- phenylpropanoylamino)propyl]hydroxypho sphinoyl] methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B. J Pharmacol Exp Ther 309 : 607 615.
    • (2004) J Pharmacol Exp Ther , vol.309 , pp. 607-615
    • Suzuki, K.1    Muto, Y.2    Fushihara, K.3    Kanemoto, K.4    Iida, H.5    Sato, E.6    Kikuchi, C.7    Matsushima, T.8    Kato, E.9    Nomoto, M.10    Yoshioka, S.11    Ishii, H.12
  • 21
    • 33846975810 scopus 로고    scopus 로고
    • A novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor (TAFIa) - Part I: Pharmacological characterization
    • Wang Y.X., Zhao L., Nagashima M., Vincelette J., Sukovich D., Li W., Subramanyam B. et al. (2007) A novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor (TAFIa) - part I: pharmacological characterization. Thromb Haemost 97 : 45 53.
    • (2007) Thromb Haemost , vol.97 , pp. 45-53
    • Wang, Y.X.1    Zhao, L.2    Nagashima, M.3    Vincelette, J.4    Sukovich, D.5    Li, W.6    Subramanyam, B.7
  • 23
    • 33746281366 scopus 로고    scopus 로고
    • Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of an uninhibited carboxypeptidase B
    • Bayes A., de la Vega M.R., Vendrell J., Aviles F.X., Jongsma M.A., Beekwilder J. (2006) Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of an uninhibited carboxypeptidase B. Insect Biochem Mol Biol 36 : 654 664.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 654-664
    • Bayes, A.1    De La Vega, M.R.2    Vendrell, J.3    Aviles, F.X.4    Jongsma, M.A.5    Beekwilder, J.6
  • 27
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • Turk B. (2006) Targeting proteases: successes, failures and future prospects. Nat Rev Drug Discov 5 : 785 799.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 785-799
    • Turk, B.1
  • 28
    • 0021327668 scopus 로고
    • CI-906 and CI-907: New orally active nonsulfhydryl angiotensin-converting enzyme inhibitors
    • Kaplan H.R., Cohen D.M., Essenburg A.D., Major T.C., Mertz T.E., Ryan M.J. (1984) CI-906 and CI-907: new orally active nonsulfhydryl angiotensin-converting enzyme inhibitors. Fed Proc 43 : 1326 1329.
    • (1984) Fed Proc , vol.43 , pp. 1326-1329
    • Kaplan, H.R.1    Cohen, D.M.2    Essenburg, A.D.3    Major, T.C.4    Mertz, T.E.5    Ryan, M.J.6
  • 29
    • 0030248565 scopus 로고    scopus 로고
    • Safety and efficacy of doxazosin in benign prostatic hyperplasia: A pooled analysis of three double-blind, placebo-controlled studies
    • Roehrborn C.G., Siegel R.L. (1996) Safety and efficacy of doxazosin in benign prostatic hyperplasia: a pooled analysis of three double-blind, placebo-controlled studies. Urology 48 : 406 415.
    • (1996) Urology , vol.48 , pp. 406-415
    • Roehrborn, C.G.1    Siegel, R.L.2
  • 30
    • 0033538529 scopus 로고    scopus 로고
    • Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme
    • Ventura S., Villegas V., Sterner J., Larson J., Vendrell J., Hershberger C.L., Aviles F.X. (1999) Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme J Biol Chem 274 : 19925 19933.
    • (1999) J Biol Chem , vol.274 , pp. 19925-19933
    • Ventura, S.1    Villegas, V.2    Sterner, J.3    Larson, J.4    Vendrell, J.5    Hershberger, C.L.6    Aviles, F.X.7
  • 31
    • 31444452744 scopus 로고
    • Automatic generation of 3D-atomic coordinates for organic molecules
    • Gasteiger J., Rudolph C., Sadowski J. (1990) Automatic generation of 3D-atomic coordinates for organic molecules. Tetrahedron Comput Methodol 3 : 537 547.
    • (1990) Tetrahedron Comput Methodol , vol.3 , pp. 537-547
    • Gasteiger, J.1    Rudolph, C.2    Sadowski, J.3
  • 33
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., Olson A.J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19 : 1639 1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 34
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50 : 760 776.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-776
  • 35
    • 33646242741 scopus 로고    scopus 로고
    • Assessing the scaffold diversity of screening libraries
    • Krier M., Bret G., Rognan D. (2006) Assessing the scaffold diversity of screening libraries. J Chem Inf Model 46 : 512 524.
    • (2006) J Chem Inf Model , vol.46 , pp. 512-524
    • Krier, M.1    Bret, G.2    Rognan, D.3
  • 36
    • 34250681353 scopus 로고    scopus 로고
    • Detailed comparison of the protein-ligand docking efficiencies of GOLD, a commercial package and ArgusLab, a licensable freeware
    • Joy S., Nair P.S., Hariharan R., Pillai M.R. (2006) Detailed comparison of the protein-ligand docking efficiencies of GOLD, a commercial package and ArgusLab, a licensable freeware. In Silico Biol 6 : 601 605.
    • (2006) In Silico Biol , vol.6 , pp. 601-605
    • Joy, S.1    Nair, P.S.2    Hariharan, R.3    Pillai, M.R.4
  • 39
    • 43049150755 scopus 로고    scopus 로고
    • Thioxophosphoranyl aryl- and heteroaryloxiranes as the representants of a new class of metallocarboxypeptidase inhibitors
    • Fernandez D., Illa O., Aviles F.X., Branchadell V., Vendrell J., Ortuno R.M. (2008) Thioxophosphoranyl aryl- and heteroaryloxiranes as the representants of a new class of metallocarboxypeptidase inhibitors. Bioorg Med Chem 16 : 4823 4828.
    • (2008) Bioorg Med Chem , vol.16 , pp. 4823-4828
    • Fernandez, D.1    Illa, O.2    Aviles, F.X.3    Branchadell, V.4    Vendrell, J.5    Ortuno, R.M.6
  • 40
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Cheng Y., Prusoff W.H. (1973) Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem Pharmacol 22 : 3099 3108.
    • (1973) Biochem Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2


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