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Volumn 7, Issue 1, 2017, Pages

Potential inhibitors designed against NDM-1 type metallo-β-lactamases: An attempt to enhance efficacies of antibiotics against multi-drug-resistant bacteria

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; BETA-LACTAMASE NDM-1;

EID: 85027967368     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-017-09588-1     Document Type: Article
Times cited : (47)

References (41)
  • 1
    • 33845379247 scopus 로고
    • Penicillin Resistance: The Chemistry of β-Lactamase Inhibition
    • Knowles, J. R. Penicillin Resistance: The Chemistry of β-Lactamase Inhibition. Acc. Chem. Res. 18, 97-104 (1985).
    • (1985) Acc. Chem. Res. , vol.18 , pp. 97-104
    • Knowles, J.R.1
  • 3
    • 84969261451 scopus 로고    scopus 로고
    • Bisthiazolidines: A substrate-mimicking scaffold as an inhibitor of the NDM-1 carbapenemase
    • Nov 13
    • González, M. M. et al. Bisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase. ACS Infect Dis. Nov 13, 1(11), 544-54 (2015).
    • (2015) ACS Infect Dis. , vol.1 , Issue.11 , pp. 544-554
    • González, M.M.1
  • 4
    • 77955917495 scopus 로고    scopus 로고
    • Emergence of a new antibiotic resistance mechanism in India, Pakistan, and the UK: A molecular, biological, and epidemiological study
    • Kumarasamy, K. K. et al. Emergence of a new antibiotic resistance mechanism in India, Pakistan, and the UK: a molecular, biological, and epidemiological study. Lancet Infect. Dis. 10, 597-602 (2010).
    • (2010) Lancet Infect. Dis. , vol.10 , pp. 597-602
    • Kumarasamy, K.K.1
  • 5
    • 77149165713 scopus 로고    scopus 로고
    • A Updated functional classification of beta-lactamases
    • Bush, K. & Jacoby, G. A Updated functional classification of beta-lactamases. Antimicrob. Agents Chemother. 54, 969-76 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 969-976
    • Bush, K.1    Jacoby, G.2
  • 7
    • 84874300806 scopus 로고    scopus 로고
    • Biochemical characterization of CTX-M-15 from Enterobacter cloacae and designing a novel non-beta-lactam-beta-lactamase inhibitor
    • Faheem, M., Rehman, M. T., Danishuddin, M. and Khan, A. U. Biochemical characterization of CTX-M-15 from Enterobacter cloacae and designing a novel non-beta-lactam-beta-lactamase inhibitor. [Erratum appears in PLoS One. 8(12) (2013).
    • (2013) PLoS One. , vol.8 , Issue.12
    • Faheem, M.1    Rehman, M.T.2    Danishuddin, M.3    Khan, A.U.4
  • 8
    • 85018471501 scopus 로고    scopus 로고
    • Metallo-β-lactamase inhibitors by bioisosteric replacement: Preparation, activity and binding
    • Skagseth, S. et al. Metallo-β-lactamase inhibitors by bioisosteric replacement: Preparation, activity and binding. Eur J Med Chem. 135, 159-173 (2017).
    • (2017) Eur J Med Chem. , vol.135 , pp. 159-173
    • Skagseth, S.1
  • 9
    • 80051979418 scopus 로고    scopus 로고
    • A structural view of the antibiotic degradation enzyme NDM-1 from a superbug
    • Guo, Y. et al. A structural view of the antibiotic degradation enzyme NDM-1 from a superbug. Protein Cell. 2, 384-394 (2011).
    • (2011) Protein Cell. , vol.2 , pp. 384-394
    • Guo, Y.1
  • 10
    • 79957618735 scopus 로고    scopus 로고
    • Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism
    • Zhang, H. & Hao, Q. Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism. FASEB J. 25, 2574-2582 (2011).
    • (2011) FASEB J. , vol.25 , pp. 2574-2582
    • Zhang, H.1    Hao, Q.2
  • 11
    • 85028012609 scopus 로고    scopus 로고
    • Structure of apo- and monometalated forms of NDM-1-A highly potent carbapenem-hydrolyzing Metallo-β-lactamase
    • Kim, Y. et al. Structure of apo- and monometalated forms of NDM-1-A highly potent carbapenem-hydrolyzing Metallo-β-lactamase. PLoS One. 6, 1-12 (2011).
    • (2011) PLoS One. , vol.6 , pp. 1-12
    • Kim, Y.1
  • 12
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis
    • Concha, N. O., Rasmussen, B. A., Bush, K. & Herzberg, O. Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. Structure. 4, 823-36 (1996).
    • (1996) Structure. , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 13
    • 0032497362 scopus 로고    scopus 로고
    • SM1, structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: Binuclear active site with features of a mononuclear enzyme
    • F. Sohi et al. structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme. Biochemistry 37(36), 12404-11 (1998).
    • (1998) Biochemistry , vol.37 , Issue.36 , pp. 12404-12411
    • Sohi, F.1
  • 15
    • 84907486093 scopus 로고    scopus 로고
    • Evaluation of inhibitory action of novel non b-lactam inhibitor against klebsiella pneumoniae carbapenemase (KPC-2)
    • Khan, A., Faheem, M., Danishuddin, M. & Khan, A. U. Evaluation of inhibitory action of novel non b-lactam inhibitor against klebsiella pneumoniae carbapenemase (KPC-2). PLoS One., doi: 10.1371/journal.pone.0108246 (2014).
    • (2014) PLoS One.
    • Khan, A.1    Faheem, M.2    Danishuddin, M.3    Khan, A.U.4
  • 16
    • 0026801518 scopus 로고
    • Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution
    • Strynadka, N. C. et al. Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution. Nature. 359, 700-705 (1992).
    • (1992) Nature. , vol.359 , pp. 700-705
    • Strynadka, N.C.1
  • 17
    • 84901748791 scopus 로고    scopus 로고
    • Insight into the binding mechanism of imipenem to human serum albumin by spectroscopic and computational approaches
    • Rehman, M. T., Shamsi, H. & Khan, A. U. Insight into the binding mechanism of imipenem to human serum albumin by spectroscopic and computational approaches. Mol. Pharm., doi: 10.1021/mp500116c (2014).
    • (2014) Mol. Pharm.
    • Rehman, M.T.1    Shamsi, H.2    Khan, A.U.3
  • 18
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink, M. R. & Ghiron, C. A. Fluorescence quenching studies with proteins. Anal. Biochem. 114, 199-227 (1981).
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 19
    • 84879494930 scopus 로고    scopus 로고
    • Study on the interaction of the epilepsy drug, zonisamide with human serum albumin (HSA) by spectroscopic and molecular docking techniques
    • Shahabadi, N., Khorshidi, A. & Moghadam, N. H. Study on the interaction of the epilepsy drug, zonisamide with human serum albumin (HSA) by spectroscopic and molecular docking techniques. Spectrochim. Acta - Part A Mol. Biomol. Spectrosc. 114, 627-632 (2013).
    • (2013) Spectrochim. Acta - Part A Mol. Biomol. Spectrosc. , vol.114 , pp. 627-632
    • Shahabadi, N.1    Khorshidi, A.2    Moghadam, N.H.3
  • 20
    • 84902531820 scopus 로고    scopus 로고
    • Understanding the fate of an anesthetic, nalorphine upon interaction with human serum albumin: A photophysical and mass-spectroscopy approach
    • Chen, Z. et al. Understanding the fate of an anesthetic, nalorphine upon interaction with human serum albumin: a photophysical and mass-spectroscopy approach. RSC Adv. 4, 25410-25419 (2014).
    • (2014) RSC Adv. , vol.4 , pp. 25410-25419
    • Chen, Z.1
  • 21
    • 84947932767 scopus 로고    scopus 로고
    • Biophysical and molecular docking insight into interaction mechanism and thermal stability of human serum albumin isoforms with a semi-synthetic water-soluble camptothecin analog irinotecan hydrochloride
    • Ishtikhar, M. et al. Biophysical and molecular docking insight into interaction mechanism and thermal stability of human serum albumin isoforms with a semi-synthetic water-soluble camptothecin analog irinotecan hydrochloride. J. Biomol. Struct. Dyn. doi: 10.1080/07391102.2015.1082504 (2015).
    • (2015) J. Biomol. Struct. Dyn.
    • Ishtikhar, M.1
  • 22
    • 77954388918 scopus 로고    scopus 로고
    • Interaction of weakly bound antibiotics neomycin and lincomycin with bovine and human serum albumin: Biophysical approach
    • Keswani, N., Choudhary, S. & Kishore, N. Interaction of weakly bound antibiotics neomycin and lincomycin with bovine and human serum albumin: biophysical approach. J Biochem 148, 71-84 (2010).
    • (2010) J Biochem , vol.148 , pp. 71-84
    • Keswani, N.1    Choudhary, S.2    Kishore, N.3
  • 23
    • 84859322059 scopus 로고    scopus 로고
    • Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor
    • Maîtrepierre, E., Sigoillot, M., Le Pessot, L. & Briand, L. Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor. Protein Expr Purif. 83(1), 75-83 (2012).
    • (2012) Protein Expr Purif. , vol.83 , Issue.1 , pp. 75-83
    • Maîtrepierre, E.1    Sigoillot, M.2    Le Pessot, L.3    Briand, L.4
  • 24
    • 84945074880 scopus 로고
    • Conjugate-direction minimization: An improved method for the refinement of macromolecules
    • Tronrud, D. E. Conjugate-direction minimization: an improved method for the refinement of macromolecules. Acta Crystallogr. Sect. A. 48, 912-916 (1992).
    • (1992) Acta Crystallogr. Sect. A. , vol.48 , pp. 912-916
    • Tronrud, D.E.1
  • 25
    • 67650500988 scopus 로고    scopus 로고
    • CHARMM: The biomolecular simulation program
    • Brooks, B. R. et al. CHARMM: The biomolecular simulation program. J. Comput. Chem. 30, 1545-1614 (2009).
    • (2009) J. Comput. Chem. , vol.30 , pp. 1545-1614
    • Brooks, B.R.1
  • 27
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris, G. & Huey, R. AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J Comput Chem. 30(16), 2785-2791 (2009).
    • (2009) J Comput Chem. , vol.30 , Issue.16 , pp. 2785-2791
    • Morris, G.1    Huey, R.2
  • 28
    • 0037310989 scopus 로고    scopus 로고
    • Clinical isolates of Enterobacteriaceae producing extended-spectrum β-lactamases: Prevalence of CTX-M-3 at a hospital in China
    • Wang, H., Kelkar, S., Wu, W., Chen, M. & Quinn, J. P. Clinical isolates of Enterobacteriaceae producing extended-spectrum β-lactamases: Prevalence of CTX-M-3 at a hospital in China. Antimicrob. Agents Chemother. 47, 790-793 (2003).
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 790-793
    • Wang, H.1    Kelkar, S.2    Wu, W.3    Chen, M.4    Quinn, J.P.5
  • 29
    • 0028922586 scopus 로고
    • Ligplot -A Program to Generate Schematic Diagrams of Protein Ligand Interactions
    • Wallace, A. C., Laskowski, R. A. & Thornton, J. M. Ligplot -a Program To Generate Schematic Diagrams of Protein Ligand Interactions. Protein Eng. 8, 127-134 (1995).
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 30
    • 46249092554 scopus 로고    scopus 로고
    • GRGMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., Van Der Spoel, D. & Lindahl, E. GRGMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447 (2008).
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 31
    • 27344454932 scopus 로고    scopus 로고
    • H. J. C. GROMACS: Fast, flexible, and free
    • Spoel, V. D. et al. H. J. C. GROMACS: Fast, flexible, and free. J. Comput. Chem. 26, 1701-1718 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1701-1718
    • Spoel, V.D.1
  • 32
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • Lindorff-Larsen, K. et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins Struct. Funct. Bioinforma. 78, 1950-1958 (2010).
    • (2010) Proteins Struct. Funct. Bioinforma. , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1
  • 33
    • 84865228751 scopus 로고    scopus 로고
    • VIP:ACPYPE - AnteChamber PYthon Parser interfacE
    • Sousa da Silva, A. W. & Vranken, W. F. VIP:ACPYPE - AnteChamber PYthon Parser interfacE. BMC Res. Notes. 5, 367 (2012).
    • (2012) BMC Res. Notes. , vol.5
    • Sousa Da Silva, A.W.1    Vranken, W.F.2
  • 37
    • 84904964377 scopus 로고    scopus 로고
    • G mmpbsa A GROMACS Tool for high-throughput MM-PBSA calculations
    • Jun 19
    • Kumari, R., Kumar, R., Lynn, A. G mmpbsa A GROMACS Tool for High-Throughput MM-PBSA Calculations. Journal of chemical information and modeling. Jun 19, 54(7), 1951-62(2014).
    • (2014) Journal of Chemical Information and Modeling. , vol.54 , Issue.7 , pp. 1951-1962
    • Kumari, R.1    Kumar, R.2    Lynn, A.3
  • 38
    • 85017449982 scopus 로고    scopus 로고
    • Application of MM/PBSA in the prediction of relative binding free energy: Re-scoring of docking hit-list
    • Dec 1
    • Kumari R, Lynn AM. Application of MM/PBSA in the prediction of relative binding free energy: Re-scoring of docking hit-list. Journal of Natural Science, Biology and Medicine. Dec 1, 2(3), 92 (2011).
    • (2011) Journal of Natural Science, Biology and Medicine. , Issue.2-3 , pp. 92
    • Kumari, R.1    Lynn, A.M.2
  • 39
    • 84862509731 scopus 로고    scopus 로고
    • Spread of carbapenemase NDM-1 producers: The situation in India and what may be proposed
    • Khan, A. U. & Nordmann, P. Spread of carbapenemase NDM-1 producers: the situation in India and what may be proposed. Scand. J. Infect. Dis. 44, 531-5 (2012).
    • (2012) Scand. J. Infect. Dis. , vol.44 , pp. 531-535
    • Khan, A.U.1    Nordmann, P.2
  • 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 WH.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(23), 3099-108 (1973).
    • (1973) Biochem Pharmacol. , vol.22 , Issue.23 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 41
    • 0028303746 scopus 로고
    • Use of the chromosomal class A β-lactamase of Mycobacterium fortuitum D316 to study potentially poor substrates and inhibitory β-lactam compounds
    • Galleni, M. et al. Use of the chromosomal class A β-lactamase of Mycobacterium fortuitum D316 to study potentially poor substrates and inhibitory β-lactam compounds. Antimicrob. Agents Chemother. 38, 1608-1614 (1994).
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1608-1614
    • Galleni, M.1


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