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Volumn 137, Issue , 2017, Pages 351-364

Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4,5-diphenyl-1H-pyrrole-3-carbonitrile as a broad spectrum metallo-β-lactamase inhibitor

Author keywords

Antibiotics resistance; Enzyme inhibition; Metallo lactamase

Indexed keywords

2 AMINOPYRROLE 1 BENZYL 4,5 DIPHENYL 1H PYRROLE 3 CARBONITRILE; ANTIBIOTIC AGENT; BETA LACTAMASE INHIBITOR; MEROPENEM; METALLO BETA LACTAMASE INHIBITOR; PYRROLE DERIVATIVE; UNCLASSIFIED DRUG; BETA LACTAMASE; ENZYME INHIBITOR; NITRILE;

EID: 85020462323     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2017.05.061     Document Type: Article
Times cited : (47)

References (57)
  • 1
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to β-Lactam Antibiotics:  compelling opportunism, compelling opportunity
    • Fisher, J.F., Meroueh, S.O., Mobashery, S., Bacterial resistance to β-Lactam Antibiotics:  compelling opportunism, compelling opportunity. Chem. Rev. 105 (2005), 395–424.
    • (2005) Chem. Rev. , vol.105 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 2
  • 3
    • 84893089095 scopus 로고    scopus 로고
    • Prospects for new antibiotics: a molecule-centered perspective
    • Walsh, C.T., Wencewicz, T.A., Prospects for new antibiotics: a molecule-centered perspective. J. Antibiot. 67 (2014), 7–22.
    • (2014) J. Antibiot. , vol.67 , pp. 7-22
    • Walsh, C.T.1    Wencewicz, T.A.2
  • 4
    • 84937003282 scopus 로고    scopus 로고
    • Synthesis and evaluation of isatin-β-thiosemicarbazones as novel agents against antibiotic-resistant Gram-positive bacterial species
    • Zhang, X.-M., Guo, H., Li, Z.-S., Song, F.-H., Wang, W.-M., Dai, H.-Q., Zhang, L.-X., Wang, J.-G., Synthesis and evaluation of isatin-β-thiosemicarbazones as novel agents against antibiotic-resistant Gram-positive bacterial species. Eur. J. Med. Chem. 101 (2015), 419–430.
    • (2015) Eur. J. Med. Chem. , vol.101 , pp. 419-430
    • Zhang, X.-M.1    Guo, H.2    Li, Z.-S.3    Song, F.-H.4    Wang, W.-M.5    Dai, H.-Q.6    Zhang, L.-X.7    Wang, J.-G.8
  • 5
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of β-lactamase inhibitors
    • Drawz, S.M., Bonomo, R.A., Three decades of β-lactamase inhibitors. Clin. Microbiol. Rev. 23 (2010), 160–201.
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 6
    • 84872871981 scopus 로고    scopus 로고
    • Metallo-β-lactamase structure and function
    • Palzkill, T., Metallo-β-lactamase structure and function. Ann. N.Y. Acad. Sci. 1277 (2013), 91–104.
    • (2013) Ann. N.Y. Acad. Sci. , vol.1277 , pp. 91-104
    • Palzkill, T.1
  • 8
    • 77149165713 scopus 로고    scopus 로고
    • Updated functional classification of β-Lactamases
    • Bush, K., Jacoby, G.A., Updated functional classification of β-Lactamases. Antimicrob. Agents Chemother. 54 (2010), 969–976.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 969-976
    • Bush, K.1    Jacoby, G.A.2
  • 12
    • 84923223411 scopus 로고    scopus 로고
    • Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262
    • Pegg, K.M., Liu, E.M., George, A.C., LaCuran, A.E., Bethel, C.R., Bonomo, R.A., Oelschlaeger, P., Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262. Protein Sci. 23 (2014), 1451–1460.
    • (2014) Protein Sci. , vol.23 , pp. 1451-1460
    • Pegg, K.M.1    Liu, E.M.2    George, A.C.3    LaCuran, A.E.4    Bethel, C.R.5    Bonomo, R.A.6    Oelschlaeger, P.7
  • 13
    • 84893809221 scopus 로고    scopus 로고
    • Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues
    • Gonzalez, L.J., Moreno, D.M., Bonomo, R.A., Vila, A.J., Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues. PLoS Pathog., 10, 2014, e1003817.
    • (2014) PLoS Pathog. , vol.10 , pp. e1003817
    • Gonzalez, L.J.1    Moreno, D.M.2    Bonomo, R.A.3    Vila, A.J.4
  • 14
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone, C., Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem. Pharmacol. 74 (2007), 1686–1701.
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 15
    • 33750624074 scopus 로고    scopus 로고
    • Metallo-β-lactamases: novel weaponry for antibiotic resistance in bacteria
    • Crowder, M.W., Spencer, J., Vila, A.J., Metallo-β-lactamases: novel weaponry for antibiotic resistance in bacteria. Acc. Chem. Res. 39 (2006), 721–728.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 721-728
    • Crowder, M.W.1    Spencer, J.2    Vila, A.J.3
  • 16
    • 84896891868 scopus 로고    scopus 로고
    • Unusual metallo-β-lactamases may constitute a new subgroup in this family of enzymes
    • Hou, C.-F.D., Phelan, E.K., Miraula, M., Ollis, D.L., Schenk, G., Mitic, N., Unusual metallo-β-lactamases may constitute a new subgroup in this family of enzymes. Am. J. Mol. Biol. 4 (2014), 11–15.
    • (2014) Am. J. Mol. Biol. , vol.4 , pp. 11-15
    • Hou, C.-F.D.1    Phelan, E.K.2    Miraula, M.3    Ollis, D.L.4    Schenk, G.5    Mitic, N.6
  • 18
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo β-Lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate Inhibitor:  binding determinants of a potent, broad-spectrum inhibitor
    • Concha, N.O., Janson, C.A., Rowling, P., Pearson, S., Cheever, C.A., Clarke, B.P., Lewis, C., Galleni, M., Frère, J.-M., Payne, D.J., Bateson, J.H., Abdel-Meguid, S.S., Crystal structure of the IMP-1 metallo β-Lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate Inhibitor:  binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39 (2000), 4288–4298.
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3    Pearson, S.4    Cheever, C.A.5    Clarke, B.P.6    Lewis, C.7    Galleni, M.8    Frère, J.-M.9    Payne, D.J.10    Bateson, J.H.11    Abdel-Meguid, S.S.12
  • 23
    • 84869237356 scopus 로고    scopus 로고
    • Characterization of an acquired subgroup B3 metallo-β-Lactamase gene, blaAIM-1, and its unique genetic context in Pseudomonas aeruginosa from Australia
    • Yong, D., Toleman, M.A., Bell, J., Ritchie, B., Pratt, R., Ryley, H., Walsh, T.R., Genetic, Biochemical, Characterization of an acquired subgroup B3 metallo-β-Lactamase gene, blaAIM-1, and its unique genetic context in Pseudomonas aeruginosa from Australia. Antimicrob. Agents Chemother. 56 (2012), 6154–6159.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 6154-6159
    • Yong, D.1    Toleman, M.A.2    Bell, J.3    Ritchie, B.4    Pratt, R.5    Ryley, H.6    Walsh, T.R.7    Genetic8    Biochemical9
  • 26
    • 80955151611 scopus 로고    scopus 로고
    • Synthesis and kinetic testing of new inhibitors for a metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
    • Mohamed, M.S., Hussein, W.M., McGeary, R.P., Vella, P., Schenk, G., Abd El-hameed, R.H., Synthesis and kinetic testing of new inhibitors for a metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa. Eur. J. Med. Chem. 46 (2011), 6075–6082.
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 6075-6082
    • Mohamed, M.S.1    Hussein, W.M.2    McGeary, R.P.3    Vella, P.4    Schenk, G.5    Abd El-hameed, R.H.6
  • 27
    • 84866631880 scopus 로고    scopus 로고
    • Synthesis and kinetic testing of tetrahydropyrimidine-2-thione and pyrrole derivatives as inhibitors of the metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
    • Hussein, W.M., Fatahala, S.S., Mohamed, Z.M., McGeary, R.P., Schenk, G., Ollis, D.L., Mohamed, M.S., Synthesis and kinetic testing of tetrahydropyrimidine-2-thione and pyrrole derivatives as inhibitors of the metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa. Chem. Biol. Drug Des. 80 (2012), 500–515.
    • (2012) Chem. Biol. Drug Des. , vol.80 , pp. 500-515
    • Hussein, W.M.1    Fatahala, S.S.2    Mohamed, Z.M.3    McGeary, R.P.4    Schenk, G.5    Ollis, D.L.6    Mohamed, M.S.7
  • 28
    • 84962239845 scopus 로고    scopus 로고
    • Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-β-lactamase IMP-1
    • Arjomandi, O.K., Hussein, W.M., Vella, P., Yusof, Y., Sidjabat, H.E., Schenk, G., McGeary, R.P., Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-β-lactamase IMP-1. Eur. J. Med. Chem. 114 (2016), 318–327.
    • (2016) Eur. J. Med. Chem. , vol.114 , pp. 318-327
    • Arjomandi, O.K.1    Hussein, W.M.2    Vella, P.3    Yusof, Y.4    Sidjabat, H.E.5    Schenk, G.6    McGeary, R.P.7
  • 32
    • 33744826819 scopus 로고    scopus 로고
    • MolDock:  a new technique for high-accuracy molecular docking
    • Thomsen, R., Christensen, M.H., MolDock:  a new technique for high-accuracy molecular docking. J. Med. Chem. 49 (2006), 3315–3321.
    • (2006) J. Med. Chem. , vol.49 , pp. 3315-3321
    • Thomsen, R.1    Christensen, M.H.2
  • 34
    • 0016612023 scopus 로고
    • Synthese von 2-Amino-3-cyano-pyrrolen
    • Roth, H.J., Eger, K., Synthese von 2-Amino-3-cyano-pyrrolen. Arch. Pharm. 308 (1975), 179–185.
    • (1975) Arch. Pharm. , vol.308 , pp. 179-185
    • Roth, H.J.1    Eger, K.2
  • 35
    • 0029896075 scopus 로고    scopus 로고
    • Chiral pyrrolo[2,3-d]pyrimidine and pyrimido[4,5-b]indole Derivatives:  Structure−Activity relationships of potent, highly stereoselective a1-adenosine receptor antagonists
    • Müller, C.E., Geis, U., Grahner, B., Lanzner, W., Eger, K., Chiral pyrrolo[2,3-d]pyrimidine and pyrimido[4,5-b]indole Derivatives:  Structure−Activity relationships of potent, highly stereoselective a1-adenosine receptor antagonists. J. Med. Chem. 39 (1996), 2482–2491.
    • (1996) J. Med. Chem. , vol.39 , pp. 2482-2491
    • Müller, C.E.1    Geis, U.2    Grahner, B.3    Lanzner, W.4    Eger, K.5
  • 36
    • 84986495375 scopus 로고
    • Selected reactions on the o-aminonitrile system of substituted pyrroles
    • Eger, K., Pfahl, J.G., Folkers, G., Roth, H.J., Selected reactions on the o-aminonitrile system of substituted pyrroles. J. Heterocycl. Chem. 24 (1987), 425–430.
    • (1987) J. Heterocycl. Chem. , vol.24 , pp. 425-430
    • Eger, K.1    Pfahl, J.G.2    Folkers, G.3    Roth, H.J.4
  • 37
    • 0242515855 scopus 로고    scopus 로고
    • Aromatic allylation via Diazotization:  variation of the allylic moiety and a short route to a benzazepine derivative
    • Ek, F., Wistrand, L.-G., Frejd, T., Aromatic allylation via Diazotization:  variation of the allylic moiety and a short route to a benzazepine derivative. J. Org. Chem. 68 (2003), 1911–1918.
    • (2003) J. Org. Chem. , vol.68 , pp. 1911-1918
    • Ek, F.1    Wistrand, L.-G.2    Frejd, T.3
  • 38
    • 0344550360 scopus 로고    scopus 로고
    • Pyrazole and isoxazole derivatives as new, potent, and selective 20-Hydroxy-5,8,11,14-eicosatetraenoic acid synthase inhibitors
    • Nakamura, T., Sato, M., Kakinuma, H., Miyata, N., Taniguchi, K., Bando, K., Koda, A., Kameo, K., Pyrazole and isoxazole derivatives as new, potent, and selective 20-Hydroxy-5,8,11,14-eicosatetraenoic acid synthase inhibitors. J. Med. Chem. 46 (2003), 5416–5427.
    • (2003) J. Med. Chem. , vol.46 , pp. 5416-5427
    • Nakamura, T.1    Sato, M.2    Kakinuma, H.3    Miyata, N.4    Taniguchi, K.5    Bando, K.6    Koda, A.7    Kameo, K.8
  • 39
    • 0027135192 scopus 로고
    • A new method for the preparation of tetrazoles from nitriles using trimethylsilylazide/trimethylaluminum
    • Huff, B.E., Staszak, M.A., A new method for the preparation of tetrazoles from nitriles using trimethylsilylazide/trimethylaluminum. Tetrahedron Lett. 34 (1993), 8011–8014.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 8011-8014
    • Huff, B.E.1    Staszak, M.A.2
  • 40
    • 0001013435 scopus 로고
    • Carbene and silicon routes as methods for the generation and dipolar cycloaddition reactions of methyl nitrile ylide
    • Padwa, A., Gasdaska, J.R., Tomas, M., Turro, N.J., Cha, Y., Gould, I.R., Carbene and silicon routes as methods for the generation and dipolar cycloaddition reactions of methyl nitrile ylide. J. Am. Chem. Soc. 108 (1986), 6739–6746.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6739-6746
    • Padwa, A.1    Gasdaska, J.R.2    Tomas, M.3    Turro, N.J.4    Cha, Y.5    Gould, I.R.6
  • 42
    • 84945251648 scopus 로고    scopus 로고
    • Diversity-oriented synthesis of calothrixins and ellipticines
    • Dethe, D.H., Murhade, G.M., Diversity-oriented synthesis of calothrixins and ellipticines. Eur. J. Org. Chem., 2014, 6953–6962.
    • (2014) Eur. J. Org. Chem. , pp. 6953-6962
    • Dethe, D.H.1    Murhade, G.M.2
  • 43
    • 84973633349 scopus 로고    scopus 로고
    • Optimization of conformational dynamics in an epistatic evolutionary trajectory
    • González, M.M., Abriata, L.A., Tomatis, P.E., Vila, A.J., Optimization of conformational dynamics in an epistatic evolutionary trajectory. Mol. Biol. Evol. 33 (2016), 1768–1776.
    • (2016) Mol. Biol. Evol. , vol.33 , pp. 1768-1776
    • González, M.M.1    Abriata, L.A.2    Tomatis, P.E.3    Vila, A.J.4
  • 44
    • 84936850143 scopus 로고    scopus 로고
    • Quantitative description of a protein fitness Landscape based on molecular features
    • Meini, M.-R., Tomatis, P.E., Weinreich, D.M., Vila, A.J., Quantitative description of a protein fitness Landscape based on molecular features. Mol. Biol. Evol. 32 (2015), 1774–1787.
    • (2015) Mol. Biol. Evol. , vol.32 , pp. 1774-1787
    • Meini, M.-R.1    Tomatis, P.E.2    Weinreich, D.M.3    Vila, A.J.4
  • 47
    • 84873823168 scopus 로고    scopus 로고
    • Evolution of broad spectrum β-Lactam resistance in an engineered metallo-β-lactamase
    • Sun, S., Zhang, W., Mannervik, B., Andersson, D.I., Evolution of broad spectrum β-Lactam resistance in an engineered metallo-β-lactamase. J. Biol. Chem. 288 (2013), 2314–2324.
    • (2013) J. Biol. Chem. , vol.288 , pp. 2314-2324
    • Sun, S.1    Zhang, W.2    Mannervik, B.3    Andersson, D.I.4
  • 49
    • 14144255746 scopus 로고    scopus 로고
    • Impact of remote mutations on metallo-β-lactamase substrate specificity: implications for the evolution of antibiotic resistance
    • Oelschlaeger, P., Mayo, S.L., Pleiss, J., Impact of remote mutations on metallo-β-lactamase substrate specificity: implications for the evolution of antibiotic resistance. Protein Sci. 14 (2005), 765–774.
    • (2005) Protein Sci. , vol.14 , pp. 765-774
    • Oelschlaeger, P.1    Mayo, S.L.2    Pleiss, J.3
  • 50
    • 33845918530 scopus 로고    scopus 로고
    • Synthesis and rearrangements of 7H-pyrrolo[3,2-e][1,2,4]triazolo[1,5-c]-and 7h-pyrrolo[3,2-e][1,2,4]triazolo[4,3-c]pyrimidines
    • Vorob'ev, E.V., Kurbatov, E.S., Krasnikov, V.V., Mezheritskii, V.V., Usova, E.V., Synthesis and rearrangements of 7H-pyrrolo[3,2-e][1,2,4]triazolo[1,5-c]-and 7h-pyrrolo[3,2-e][1,2,4]triazolo[4,3-c]pyrimidines. Russ. Chem. Bull. 55 (2006), 1492–1497.
    • (2006) Russ. Chem. Bull. , vol.55 , pp. 1492-1497
    • Vorob'ev, E.V.1    Kurbatov, E.S.2    Krasnikov, V.V.3    Mezheritskii, V.V.4    Usova, E.V.5
  • 52
    • 64349087922 scopus 로고    scopus 로고
    • Synthesis of nickel-chelating fluorinated lipids for protein monolayer crystallizations
    • Hussein, W.M., Ross, B.P., Landsberg, M.J., Lévy, D., Hankamer, B., McGeary, R.P., Synthesis of nickel-chelating fluorinated lipids for protein monolayer crystallizations. J. Org. Chem. 74 (2009), 1473–1479.
    • (2009) J. Org. Chem. , vol.74 , pp. 1473-1479
    • Hussein, W.M.1    Ross, B.P.2    Landsberg, M.J.3    Lévy, D.4    Hankamer, B.5    McGeary, R.P.6
  • 53
    • 0003760238 scopus 로고
    • Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems
    • Wiley
    • Segel, I.H., Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. 1993, Wiley.
    • (1993)
    • Segel, I.H.1
  • 56
    • 84871201908 scopus 로고    scopus 로고
    • Activity of carbapenems with ME1071 (disodium 2,3-diethylmaleate) against Enterobacteriaceae and Acinetobacter spp. with carbapenemases, including NDM enzymes
    • Livermore, D.M., Mushtaq, S., Morinaka, A., Ida, T., Maebashi, K., Hope, R., Activity of carbapenems with ME1071 (disodium 2,3-diethylmaleate) against Enterobacteriaceae and Acinetobacter spp. with carbapenemases, including NDM enzymes. J. Antimicrob. Chemother. 68 (2013), 153–158.
    • (2013) J. Antimicrob. Chemother. , vol.68 , pp. 153-158
    • Livermore, D.M.1    Mushtaq, S.2    Morinaka, A.3    Ida, T.4    Maebashi, K.5    Hope, R.6


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