Issue

Vol. 31 No. 10 (2019): Vol 31 Issue 10

Copyright (c) 2019 AJC

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Synthesis, Characterization and in vitro Antimicrobial Evaluation of Chalconeimine Derivatives as Potential Inhibitors against Enzymes Produced from S. aureus: A Computational Approach

https://doi.org/10.14233/ajchem.2019.22028
B. Prithivirajan
Research and Development Centre, Bharathiar University, Coimbatore-641046, India
M. Jebastin Sonia Jas
Research and Development Centre, Bharathiar University, Coimbatore-641046, India & Department of Chemistry, IFET College of Engineering, Villupuram-605108, India
G. Marimuthu
Department of Chemistry, Swami Dayananda College of Arts and Science, Manjakkudi-612610, India

Corresponding Author(s) : G. Marimuthu

gmarimuuthu@gmail.com

Asian Journal of Chemistry, Vol. 31 No. 10 (2019): Vol 31 Issue 10

Abstract

(Z)-1-(Benzo[d][1,3]dioxol-5-yl)-3-(4-(difluoromethoxy)-3-hydroxyphenyl)prop-2-en-1-one hydrazone derivatives pronounced in this manuscript represents a new collection of antibacterial agents in addition to the DNA gyrase inhibitors. Efforts had been made to synthesize those chalcone-hydrazone derivatives (4a-e) in good yields. The literature survey confirms that nano-ZnO as heterogeneous catalyst has obtained big interest because of its ecofriendly nature and has been explored as a effective catalyst for several organic ameliorations. Subsequently, induced by way of these observations and in continuation to our interest in organic synthesis with using nanocatalyst. in vitro Antibacterial activity has been evaluated towards Gram-positive and Gram-negative bacterial strains for all compounds. So one can discover the affinity to bacterial proteins docking have a look at have been carried out for 5 synthesized derivatives, antibiotic drug and co-crystallized ligands with special mechanism of action DNA gyrase B and methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTAN) the usage of AutoDock 4.

Keywords

Hydrazone Chalcone Antibacterial Docking DNA gyrase B Methylthioadenosine
Prithivirajan, B., Sonia Jas, M. J., & Marimuthu, G. (2019). Synthesis, Characterization and in vitro Antimicrobial Evaluation of Chalconeimine Derivatives as Potential Inhibitors against Enzymes Produced from S. aureus: A Computational Approach. Asian Journal of Chemistry, 31(10), 2157–2164. https://doi.org/10.14233/ajchem.2019.22028
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
References
  1. C.L. Miranda, J.F. Stevens, V. Ivanov, M. McCall, B. Frei, M.L. Deinzer and D.R. Buhler, J. Agric. Food Chem., 48, 3876 (2000); https://doi.org/10.1021/jf0002995.
  2. M. Liu, P. Wilairat and L.M. Go, J. Med. Chem., 44, 4443 (2001); https://doi.org/10.1021/jm0101747.
  3. G.S. Viana, M.A. Bandeira and F. Matos, Phytomedicine, 10, 189 (2003); https://doi.org/10.1078/094471103321659924.
  4. V. Rangari, V.N. Gupta and C.K. Atal, Indian J. Pharm. Sci., 52, 158 (1990).
  5. F. Epifano, S. Genovese, L. Menghini and M. Curini, Phytochemistry, 68, 939 (2007); https://doi.org/10.1016/j.phytochem.2007.01.019.
  6. Nissan Chemical Industries Ltd., Japan Kokai Tokkyo Koho Japan Patent 58,08,035 (1983); Chem. Abstr., 98, 178947a (1983).
  7. K. Bowden, P.A. Dal and C.K. Shah, J. Chem. Res. (S), 12, 2801 (1990); Chem. Abstr., 114, 160570m (1991).
  8. V.M. Gaurav and D.B. Ingle, J. Indian Chem., 25B, 868 (1986).
  9. L.C. Manchester, B. Poeggeler, F.L. Alvares, G.B. Ogden and R.J. Reiter, Cell Mol. Biol. Res., 41, 391 (1995).
  10. H.W. Boucher, G.H. Talbot, J.S. Bradley, J.E. Edwards, D. Gilbert, L.B. Rice, M. Scheld, B. Spellberg and J. Bartlett, Clin. Infect. Dis., 48, 1 (2009); https://doi.org/10.1086/595011.
  11. J. Kluytmans, A. van Belkum and H. Verbrugh, Clin. Microbiol. Rev., 10, 505 (1997); https://doi.org/10.1128/CMR.10.3.505.
  12. M.J. Kuehnert, H.A. Hill, B.A. Kupronis, J.I. Tokars, S.L. Solomon and D.B. Jernigan, Emerg. Infect. Dis., 11, 868 (2005); https://doi.org/10.3201/eid1106.040831.
  13. R.M. Klevens, M.A. Morrison, J. Nadle, S. Petit, K. Gershman, S. Ray, L.H. Harrison, R. Lynfield, G. Dumyati, J.M. Townes, A.S. Craig, E.R. Zell, G.E. Fosheim, L.K. McDougal, R.B. Carey and S.K. Fridkin, JAMA, 298, 1763 (2007); https://doi.org/10.1001/jama.298.15.1763.
  14. M. Diefenbeck, U. Mennenga, P. Guckel, A.H. Tiemann, T. Muckley and G.O. Hofmann, Z. Orthop. Unfall., 149, 336 (2011); https://doi.org/10.1055/s-0030-1270952.
  15. J.L. Wang, S.P. Tseng, P.R. Hsueh and K. Hiramatsu, Taiwan Emerg. Infect. Dis., 10, 1702 (2004).
  16. J. Ruiz, J. Antimicrob. Chemother., 51, 1109 (2003); https://doi.org/10.1093/jac/dkg222.
  17. J.A. Sutcliffe, T.D. Gootz and J.F. Barrett, Antimicrob. Agents Chemother., 33, 2027 (1989).
  18. C.B. Anfinsen, J. Edsall and F. Richards, Advances in Protein Chemistry, Academic Press: (Google eBook), vol. 38 (1986).
  19. N. Parveen and K.A. Cornell, Mol. Microbiol., 79, 7 (2011); https://doi.org/10.1111/j.1365-2958.2010.07455.x.
  20. K.K.W. Siu, J.E. Lee, G.D. Smith, C. Horvatin-Mrakovcic and P.L. Howell, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 64, 343 (2008); https://doi.org/10.1107/S1744309108009275.
  21. J.W. Miller, M.R. Nadeau, J. Smith, D. Smith and J. Selhub, Biochem. J., 298, 415 (1994); https://doi.org/10.1042/bj2980415.
  22. S. Schauder, K. Shokat, M.G. Surette and B.L. Bassler, Mol. Microbiol., 41, 463 (2001); https://doi.org/10.1046/j.1365-2958.2001.02532.x.
  23. X. Chen, S. Schauder, N. Potier, A. Van Dorsselaer, I. Pelczer, B.L. Bassler and F.M. Hughson, Nature, 415, 545 (2002); https://doi.org/10.1038/415545a.
  24. J.H. Clark, Pure Appl. Chem., 73, 103 (2001); https://doi.org/10.1351/pac200173010103.
  25. V.J. Mohanraj and Y. Chen, Trop. J. Pharm. Res., 5, 561 (2006); https://doi.org/10.4314/tjpr.v5i1.14634.
  26. G.M. Morris, R. Huey, W. Lindstrom, M.F. Sanner, R.K. Belew, D.S. Goodsell and A.J. Olson, J. Comput. Chem., 30, 2785 (2009); https://doi.org/10.1002/jcc.21256.
  27. O. Trott and A.J. Olson, J. Comput. Chem., 31, 455 (2010); https://doi.org/10.1002/jcc.21334.
  28. F.C. Bernstein, T.F. Koetzle, G.J.B. Williams, E.F. Meyer Jr., M.D. Brice, J.R. Rodgers, O. Kennard, T. Shimanouchi and M. Tasumi, J. Mol. Biol., 112, 535 (1977); https://doi.org/10.1016/S0022-2836(77)80200-3.
  29. D. Kaushik, S.A. Khan, G. Chawla and S. Kumar, Eur. J. Med. Chem., 45, 3943 (2010); https://doi.org/10.1016/j.ejmech.2010.05.049.
  30. S. Han, F.-F. Zhang, X. Xie and J.-Z. Chen, Eur. J. Med. Chem., 74, 73 (2014); https://doi.org/10.1016/j.ejmech.2013.12.018.
  31. S.-Y. Pung, W.-P. Lee and A. Aziz, Int. J. Inorg. Chem., 2012, 1 (2012); https://doi.org/10.1155/2012/608183.
  32. B.D. Culity, Elements of X-Ray Diffraction, Addison-Wesley: USA, edn 2 (1987).
  33. P. Bhattacharyya, K. Pradhan, S. Paul and A.R. Das, Tetrahedron Lett., 53, 4687 (2012); https://doi.org/10.1016/j.tetlet.2012.06.086.
  34. S. Farhadi and Z. Babazadeh Maleki, Acta Chim. Slov., 53, 72 (2006).
  35. K.A. Ohemeng, B.L. Podlogar, V.N. Nguyen, J.I. Bernstein, H.M. Krause, J.J. Hilliard and J.F. Barrett, J. Med. Chem., 40, 3292 (1997); https://doi.org/10.1021/jm9701583.
Read More
Author biographies is not available.
Download
PDF
Statistic
Read Counter : 0 Download : 0