NOTA analogue: A first dithiocarbamate inhibitor of metallo-β-lactamases

Bioorganic and Medicinal Chemistry Letters

Volumn 28, Issue 2, 2018, Pages 214-221

  Zhang, En ^a,c   Wang, Ming Ming ^a   Huang, Shu Chao ^b   Xu, Shuai Min ^a   Cui, De Yun ^a   Bo, Yuan Li ^a   Bai, Peng Yan ^a   Hua, Yong Gang ^a   Xiao, Chun Ling ^b   Qin, Shangshang ^a,c  

^a ZHENGZHOU UNIVERSITY   (China)

^b INSTITUTE OF MEDICINAL BIOTECHNOLOGY   (China)

^c Department of Pharmaceutics   (China)

Author keywords

Antibiotic resistance; Cyclic dithiocarbamate; Metallo lactamase; NDM 1 inhibitor

Indexed keywords

DITHIOCARBAMIC ACID DERIVATIVE; ENZYME INHIBITOR; MEROPENEM; METALLO BETA LACTAMASE; SODIUM 1,4,7 TRIAZONANE 1,4,7 TRIS(CARBOXYLODITHIOATE); UNCLASSIFIED DRUG; ZINC ION; 1,4,7-TRIAZACYCLONONANE-N,N',N''-TRIACETIC ACID; ANTIINFECTIVE AGENT; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; HETEROCYCLIC COMPOUND;

ANTIBACTERIAL ACTIVITY; ARTICLE; CANCER INHIBITION; CITROBACTER FREUNDII; CONTROLLED STUDY; CYTOTOXICITY; DRUG EFFICACY; DRUG IDENTIFICATION; DRUG STRUCTURE; DRUG SYNTHESIS; ENZYME INHIBITION; ESCHERICHIA COLI; FLUORESCENCE MICROSCOPY; GENETIC RESISTANCE; HELA CELL LINE; HUMAN; HUMAN CELL; IN VITRO STUDY; KLEBSIELLA PNEUMONIAE; NONHUMAN; PROTEUS MIRABILIS; CELL SURVIVAL; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; DRUG EFFECTS; METABOLISM; MICROBIAL SENSITIVITY TEST; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

ANTI-BACTERIAL AGENTS; BETA-LACTAMASE INHIBITORS; BETA-LACTAMASES; CELL SURVIVAL; CITROBACTER FREUNDII; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; HELA CELLS; HETEROCYCLIC COMPOUNDS; HUMANS; KLEBSIELLA PNEUMONIAE; MICROBIAL SENSITIVITY TESTS; MOLECULAR STRUCTURE; PROTEUS MIRABILIS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 85038830387     PISSN: 0960894X     EISSN: 14643405     Source Type: Journal    
DOI: 10.1016/j.bmcl.2017.10.074     Document Type: Article

References (44)

1. Van Boeckel, T.P., Gandra, S., Ashok, A., et al. Global antibiotic consumption 2000 to 2010: an analysis of national pharmaceutical sales data. Lancet Infect Dis, 14, 2014, 742.
2. Van Boeckel, Morens, David M., Folkers, G.K., Fauci, A.S., The challenge of emerging and re-emerging infectious diseases. Nature, 430, 2004, 242.
3. Livermore, D.M., Discovery research: the scientific challenge of finding new antibiotics. J Antimicrob Chemother, 66, 2011, 1941.
4. Papp-Wallace, K.M., Endimiani, A., Taracila, M.A., Bonomo, R.A., Carbapenems: past, present, and future. Antimicrob Agents Chemother, 55, 2011, 4943.
5. Fisher, Jed F., Meroueh, Samy O., Mobashery, S., Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity. Chem Rev, 105, 2005, 395.
6. Pitout, J.D.D., Laupland, K.B., Extended-spectrum β-lactamase-producing Enterobacteriaceae: an emerging public-health concern. Lancet Infect Dis, 8, 2008, 159.
7. Nordmann, P., Naas, T., Poirel, L., Global spread of carbapenemase-producing Enterobacteriaceae. Emerg Infect Dis, 17, 2011, 1791.
8. Deshpande, P., Rodrigues, C., Shetty, A., Kapadia, F., Hedge, A., Soman, R., New Delhi Metallo-lactamase (NDM-1) in enterobacteriaceae: treatment options with carbapenems compromised. J Assoc Physicians India, 58, 2010, 147.
9. Zhanel, G.G., Wiebe, R., Dilay, L., et al. Comparative review of the carbapenems. Drugs, 67, 2007, 1027.
10. Senda, K., Arakawa, Y., Nakashima, K., et al. Multifocal outbreaks of metallo-beta-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum beta-lactams, including carbapenems. Antimicrob Agents Chemother, 40, 1996, 349.
11. Drawz, S.M., Bonomo, R.A., Three decades of beta-lactamase inhibitors. Clin Microbiol Rev, 23, 2010, 160.
12. Docquier, J.D., On functional and structural heterogeneity of VIM-type metallo-beta-lactamases. J Antimicrob Chemother, 51, 2003, 257.
13. Bush, K., Jacoby, G.A., Updated functional classification of beta-lactamases. Antimicrob Agents Chemother, 54, 2010, 969.
14. Lienard, B.M., Garau, G., Horsfall, L., et al. Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols. Org Biomol Chem, 6, 2008, 2282.
15. Fast, W., Sutton, L.D., Metallo-beta-lactamase: inhibitors and reporter substrates. Biochim Biophys Acta, 1834, 2013, 1648.
16. Bush, K., Proliferation and significance of clinically relevant beta-lactamases. Ann NY Acad Sci, 1277, 2013, 84.
17. Garcia-Saez, I., Hopkins, J., Papamicael, C., et al. The 1.5-a structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril. J Biol Chem, 278, 2003, 23868.
18. Yusof, Y., Tan, D.T., Arjomandi, O.K., Schenk, G., McGeary, R.P., Captopril analogues as metallo-beta-lactamase inhibitors. Bioorg Med Chem Lett, 26, 2016, 1589.
19. Toney, J.H., Hammond, G.G., Fitzgerald, P.M., et al. Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-β-lactamase. J Biol Chem, 276, 2001, 31913.
20. Ishii, Y., Eto, M., Mano, Y., Tateda, K., Yamaguchi, K., In vitro potentiation of carbapenems with ME1071, a novel metallo-β-lactamase inhibitor, against metallo-β-lactamase-producing Pseudomonas aeruginosa clinical isolates. Antimicrob Agents Chemother, 54, 2010, 3625.
21. van Berkel, S.S., Brem, J., Rydzik, A.M., et al. Assay platform for clinically relevant metallo-beta-lactamases. J Med Chem, 56, 2013, 6945.
22. Buynak, J.D., β-Lactamase inhibitors: a review of the patent literature (2010–2013). Expert Opin Ther Pat, 23, 2013, 1469.
23. Vella, P., Hussein, W.M., Leung, E.W., et al. The identification of new metallo-beta-lactamase inhibitor leads from fragment-based screening. Bioorg Med Chem Lett, 21, 2011, 3282.
24. King, A.M., Reid-Yu, S.A., Wang, W., et al. Aspergillomarasmine A overcomes metallo-beta-lactamase antibiotic resistance. Nature, 510, 2014, 503.
25. Zhang, Y., Hong, H., Engle, J.W., et al. Positron emission tomography imaging of CD105 expression with a 64 Cu-labeled monoclonal antibody: NOTA is superior to DOTA. PLoS One, 6, 2011, e28005.
26. Boros, E., Ferreira, C.L., Cawthray, J.F., et al. Acyclic chelate with ideal properties for 68Ga PET imaging agent elaboration. J Am Chem Soc, 132, 2010, 15726.
27. Ebenhan, T., Zeevaart, J.R., Venter, J.D., et al. Preclinical evaluation of 68Ga-labeled 1,4,7-triazacyclononane-1,4,7-triacetic acid-ubiquicidin as a radioligand for PET infection imaging. J Nucl Med, 55, 2014, 308.
28. Somboro, A.M., Tiwari, D., Bester, L.A., et al. NOTA: a potent metallo-beta-lactamase inhibitor. J Antimicrob Chemother, 70, 2015, 1594.
29. Klingler, F.M., Wichelhaus, T.A., Frank, D., et al. Approved drugs containing thiols as inhibitors of metallo-beta-lactamases: strategy to combat multidrug-resistant bacteria. J Med Chem, 58, 2015, 3626.
30. Falconer, S.B., Reid-Yu, S.A., King, A.M., et al. Zinc chelation by a small-molecule adjuvant potentiates meropenem activity in vivo against NDM-1-producing Klebsiella pneumoniae. ACS Infect Dis, 1, 2015, 533.
31. Franz, K.J., Clawing back: broadening the notion of metal chelators in medicine. Curr Opin Chem Biol, 17, 2013, 143.
32. Whitnall, M., Howard, J., Ponka, P., Richardson, D.R., A class of iron chelators with a wide spectrum of potent antitumor activity that overcomes resistance to chemotherapeutics. Proc Natl Acad Sci USA, 103, 2006, 14901.
33. Perez, L.R., Franz, K.J., Minding metals: tailoring multifunctional chelating agents for neurodegenerative disease. Dalton Trans, 39, 2010, 2177.
34. Duan, Y.C., Ma, Y.C., Zhang, E., et al. Design and synthesis of novel 1,2,3-triazole-dithiocarbamate hybrids as potential anticancer agents. Eur J Med Chem, 62, 2013, 11.
35. Zhang, E., Jiao, W.-W., Wang, S., et al. Design, synthesis, and preliminary evaluation of the biological activity of dithiocarbamate-3-epi-jaspine B hybrids. Med Chem Res, 25, 2016, 3011.
36. Carta, F., Akdemir, A., Scozzafava, A., Masini, E., Supuran, C.T., Xanthates and trithiocarbonates strongly inhibit carbonic anhydrases and show antiglaucoma effects in vivo. J Med Chem, 56, 2013, 4691.
37. Shen, L., Ye, Y.-H., Wang, X.-T., et al. Structure and total synthesis of aspernigerin: a novel cytotoxic endophyte metabolite. Chem Eur J, 12, 2006, 4393.
38. Syrjänen, L., Tolvanen, M.E.E., Hilvo, M., et al. Characterization, bioinformatic analysis and dithiocarbamate inhibition studies of two new α-carbonic anhydrases, CAH1 and CAH2, from the fruit fly Drosophila melanogaster. Bioorg Med Chem, 21, 2013, 1516.
39. Li, R.-T., Cai, M.-S., Convenient synthesis of 1,4-di-(alkyldithioate) piperazines. Synth Commun, 29, 1999, 65.
40. Crystallographic data for 7 was deposited at the Cambridge Crystallographic Data Centre (deposition no. CCDC-1496928). Copies of these data can be obtained free of charge www.ccdc.cam.ac.uk.
41. Doyle, D., Peirano, G., Lascols, C., Lloyd, T., Church, D.L., Pitout, J.D., Laboratory detection of Enterobacteriaceae that produce carbapenemases. J Clin Microbiol, 50, 2012, 3877.
42. Ling, L.L., Schneider, T., Peoples, A.J., et al. A new antibiotic kills pathogens without detectable resistance. Nature, 517, 2015, 455.
43. Hoque, J., Konai, M.M., Gonuguntla, S., et al. Membrane active small molecules show selective broad spectrum antibacterial activity with no detectable resistance and eradicate biofilms. J Med Chem, 58, 2015, 5486.
44. Hoque, J., Konai, M.M., Samaddar, S., et al. Selective and broad spectrum amphiphilic small molecules to combat bacterial resistance and eradicate biofilms. Chem Commun, 51, 2015, 13670.