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Vol. 31 No. 12 (2019): Vol 31 Issue 12

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in silico Anti-Cholinestarase Activity of Flavonoids: A Computational Approach

https://doi.org/10.14233/ajchem.2019.22153
Niraj Kumar Singh
Division of Pharmacology, Institute of Pharmaceutical Research, GLA University, Mathura-281406, India
Somdutt Mujwar
Division of Pharmaceutical Chemistry, Institute of Pharmaceutical Research, GLA University, Mathura-281406, India
Debapriya Garabadu
Division of Pharmacology, Institute of Pharmaceutical Research, GLA University, Mathura-281406, India

Asian Journal of Chemistry, Vol. 31 No. 12 (2019): Vol 31 Issue 12

Abstract

In the present study, a computational approach has been designed to evaluate the potential anti-cholinesterase activity of derivatives of flavonoids. Molecular docking studies is performed for the 9 flavonoids against the human acetylcholine (ACh) enzyme to evaluate their binding affinity for having anti-alzheimer activity. All the 9 flavonoid compounds exhibited strong binding affinity that promises potent inhibition of human acetylcholine enzyme. Potential binding affinity of all the flavonoids against human acetylcholine enzyme confirms their possible mechanism of action by using AutoDock based molecular docking simulation technique. Thus, these flavonoid compounds could be presumed to be potential anti-cholinesterase drugs.

Keywords

Flavonoids Alzheimer Anticholinesterase
Singh, N. K., Mujwar, S., & Garabadu, D. (2019). in silico Anti-Cholinestarase Activity of Flavonoids: A Computational Approach. Asian Journal of Chemistry, 31(12), 2859–2864. https://doi.org/10.14233/ajchem.2019.22153
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References
  1. L.C. Dos Santos Picanco, P.F. Ozela, M. de Fatima de Brito-Brito, A.A. Pinheiro, E.C. Padilha, F.S. Braga, C.H.T. de Paula da Silva, C.B.R. Dos Santos, J.M.C. Rosa and L.I. da Silva Hage-Melim, Curr. Med. Chem., 25, 3141 (2018)https://doi.org/10.2174/0929867323666161213101126.
  2. I.G. Onyango, J. Dennis and S.M. Khan, Aging Dis., 7, 201 (2016); https://doi.org/10.14336/AD.2015.1007.
  3. H.Q. Sun, X. Zhang, W.J. Huang and W.W. Chen, Eur. Rev. Med. Pharmacol. Sci., 20, 1903 (2016).
  4. H. Robert and M.D. Howland, J. Psychosoc. Ment. Health Serv., 49, 13 (2011).
  5. M.R. Cesarone, G. Laurora, A. Ricci, G. Belcaco and P. Pomante, J. Vas. Disease, 21, 76 (1992).
  6. M. Lutz, E. Fuentes, F. Ávila, M. Alarcón and I. Palomo, Molecules, 24, 366 (2019); https://doi.org/10.3390/molecules24020366.
  7. X. Han, T. Shen and H. Lou, Int. J. Mol. Sci., 8, 950 (2007); https://doi.org/10.3390/i8090950.
  8. C. Kandaswami and E. Middleton, Adv. Exp. Med. Biol., 366, 351 (1994); https://doi.org/10.1007/978-1-4615-1833-4_25.
  9. D. Tungmunnithum, A. Thongboonyou, A. Pholboon and A. Yangsabai, Medicines, 5, 93 (2018); https://doi.org/10.3390/medicines5030093.
  10. J. Duarte, F. Pérez-Vizcaíno, A. Zarzuelo, J. Jiménez and J. Tamargo, Eur. J. Pharmacol., 239, 1 (1993); https://doi.org/10.1016/0014-2999(93)90968-N.
  11. C.A. Rice-Evans, N.J. Miller and G. Paganga, Free Radic. Biol. Med., 20, 933 (1996); https://doi.org/10.1016/0891-5849(95)02227-9.
  12. A.J. Elliott, S.A. Scheiber, C. Thomas and R.S. Pardini, Biochem. Pharmacol., 44, 1603 (1992).
  13. W.S. Chang, Y.J. Lee, F.J. Lu and H.C. Chiang, Anticancer Res., 13, 6A (1993).
  14. Y. Hanasaki, S. Ogawa and S. Fukui, Free Radic. Biol. Med., 16, 6845 (1994); https://doi.org/10.1016/0891-5849(94)90202-X.
  15. J.L. Cotelle Bernier, J.P. Henichart, J.P. Catteau, E. Gaydou and J.C. Wallet, Free Radic. Biol. Med., 13, 3 (1992).
  16. G. Chen, M. Griffin, J. Lee Poyer, P.B. McCay and D.W.A. Bourne, Free Radic. Biol. Med., 9, 93 (1990); https://doi.org/10.1016/0891-5849(90)90110-5.
  17. M. Erben-Russ, C. Michel, W. Bors and M. Saran, J. Phys. Chem., 91, 2362 (1987); https://doi.org/10.1021/j100293a033.
  18. S.V. Jovanovic, S. Steenken, M. Tosic, B. Marjanovic and M.G. Simic, J. Am. Chem. Soc., 116, 4846 (1994); https://doi.org/10.1021/ja00090a032.
  19. C.G. Frag, V.S. Martino, G.E. Ferraro, J.D. Coussio and A. Boveris, Biochem. Pharmacol., 36, 5 (1987).
  20. A. Negre-Salvayre, Y. Alomar, M. Troly and R. Salvayre, Biochim. Biophys. Acta, 1096, 291 (1991); https://doi.org/10.1016/0925-4439(91)90065-H.
  21. J. Terao, M. Piskula and Q. Yao, Arch. Biochem. Biophys., 308, 278 (1994); https://doi.org/10.1006/abbi.1994.1039.
  22. H. Mangiapane, J. Thomson, A. Salter, S. Brown, G.D. Bell and D.A. White, Biochem. Pharmacol., 43, 445 (1992); https://doi.org/10.1016/0006-2952(92)90562-W.
  23. C.V. De Whalley, S.M. Rankin, J.R. Hoult, W. Jessup and D.S. Leake, Biochem. Pharmacol., 39, 1743 (1990); https://doi.org/10.1016/0006-2952(90)90120-A.
  24. R.J. Nijveldt, E. van Nood, D.E. van Hoorn, P.G. Boelens, K. van Norren and P.A. van Leeuwen, Am. J. Clin. Nutr., 74, 418 (2001); https://doi.org/10.1093/ajcn/74.4.418.
  25. T. Fotsis, M.S. Pepper, E. Aktas, S. Breit, S. Rasku, H. Adlercreutz, K. Wahala, R. Montesano and L. Schweigerer, Cancer Res., 57, 14 (1997).
  26. D.H. Paper, Planta Med., 64, 686 (1998); https://doi.org/10.1055/s-2006-957559.
  27. M.D. Losiewicz, B.A. Carlson, G. Kaur, E.A. Sausville and P.J. Worland, Biochem. Biophys. Res. Commun., 201, 589 (1994); https://doi.org/10.1006/bbrc.1994.1742.
  28. C. Rice-Evans, N.J. Miller, G.P. Bolwell, P.M. Bramley and J.B. Pridham, Free Radic. Res., 22, 375 (1995); https://doi.org/10.3109/10715769509145649.
  29. C. Castelluccio, G. Paganga, N. Melikian, G. Paul Bolwell, J. Pridham, J. Sampson and C. Rice-Evans, FEBS Lett., 368, 188 (1995); https://doi.org/10.1016/0014-5793(95)00639-Q.
  30. B. Rosengarten, S. Paulsen, S. Molnar, R. Kaschel, B. Gallhofer and M. Kaps, J. Neurol., 253, 58 (2006); https://doi.org/10.1007/s00415-005-0926-5.
  31. B. Matharu, G. Gibson, R. Parsons, T.N. Huckerby, S.A. Moore, L.J. Cooper, R. Millichamp, D. Allsop and B. Austen, J. Neurol. Sci., 280, 49 (2009); https://doi.org/10.1016/j.jns.2009.01.024.
  32. H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov and P.E. Bourne, Nucleic Acids Res., 28, 235 (2000); https://doi.org/10.1093/nar/28.1.235.
  33. M.C. Franklin, M.J. Rudolph, C. Ginter, M.S. Cassidy and J. Cheung, Proteins, 84, 1246 (2016); https://doi.org/10.1002/prot.25073.
  34. D.S. Goodsell, G.M. Morris and A.J. Olson, J. Mol. Recognit., 9, 1 (1996); https://doi.org/10.1002/(SICI)1099-1352(199601)9:1<1::AID-JMR241>3.0.CO;2-6.
  35. W.L. DeLano, CCP4 Newsletter On Protein Crystallography, 40, 1 (2002).
  36. E.F. Pettersen, T.D. Goddard, C.C. Huang, G.S. Couch, D.M. Greenblatt, E.C. Meng and T.E. Ferrin, J. Comput. Chem., 25, 1605 (2004); https://doi.org/10.1002/jcc.20084.
  37. S. Mujwar and K.R. Pardasani, J. Med. Imaging Health Infor., 5, 1 (2015); https://doi.org/10.1166/jmihi.2015.1357.
  38. A.N. Panche, A.D. Diwan and S.R. Chandra, J. Nutr. Sci., 5, e47 (2016); https://doi.org/10.1017/jns.2016.41.
  39. G. Gattuso, D. Barreca, C. Gargiulli, U. Leuzzi and C. Caristi, Molecules, 12, 1641 (2007); https://doi.org/10.3390/12081641.
  40. S. Bhattacharya, Pharmacogn. Res., 3, 147 (2011); https://doi.org/10.4103/0974-8490.81966.
  41. J.C. Stoclet and V. Schini-Kerth, Ann. Pharm. Fr., 69, 78 (2011); https://doi.org/10.1016/j.pharma.2010.11.004.
  42. K. Herrmann, Int. J. Food Sci. Technol., 11, 433 (1976); https://doi.org/10.1111/j.1365-2621.1976.tb00743.x.
  43. J. Kuhnau, World Rev. Nutr. Diet., 24, 117 (1976); https://doi.org/10.1159/000399407.
  44. K. Herrmann and C.W. Nagel, Crit. Rev. Food Sci. Nutr., 28, 315 (1989); https://doi.org/10.1080/10408398909527504.
  45. S.V. Jovanovic, I. Jankovic and L. Josimovic, J. Am. Chem. Soc., 114, 9018 (1992); https://doi.org/10.1021/ja00049a037.
  46. Y. Xie, W. Yang, F. Tang, X. Chen and L. Ren, Curr. Med. Chem., 22, 132 (2015); https://doi.org/10.2174/0929867321666140916113443.
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