Issue

Vol. 36 No. 5 (2024): Vol 36 Issue 5, 2024

Creative Commons License

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

Synthesis and Evaluation of Aminothiazole Hybrids as Potential Acetylcholinesterase Inhibitors

https://doi.org/10.14233/ajchem.2024.31241
Arti Soni
Department of Pharmaceutical Sciences, Guru Jambheshwar University of Science and Technology, Hisar-125001, India
https://orcid.org/0000-0002-5912-2518
Ashwani Kumar
Department of Pharmaceutical Sciences, Guru Jambheshwar University of Science and Technology, Hisar-125001, India
https://orcid.org/0000-0002-8966-3569
Vivek Kumar
Janta College of Pharmacy, Butana, Sonipat-131001, India
https://orcid.org/0000-0002-6514-8474
Ravi Rawat
School of Health Sciences & Technology, UPES University, Dehradun-248007, India
https://orcid.org/0000-0001-6510-1046
Volkan Eyupoglu
Department of Chemistry, Cankiri Karatekin University, Cankiri-18100, Turkey
https://orcid.org/0000-0001-9108-3558

Corresponding Author(s) : Arti Soni

artisoni26@gmail.com

Asian Journal of Chemistry, Vol. 36 No. 5 (2024): Vol 36 Issue 5, 2024

Abstract

This study aimed to synthesize aminothiazole derivatives with 1,3,4-oxadiazole moiety and evaluated their acetylcholinesterase (AChE) and antioxidant activity in order to check their potency against Alzheimer's disease. Inhibition screening against AChE indicated that  synthesized derivatives expressed well to moderate AChE inhibitory activity in vitro. Of the examined synthetic compounds (3a-i), compound 3d expressed the best inhibition with IC50-0.35 µM. The antioxidant activity of all the synthesized compounds was also  analyzed by the DPPH assay. Finally, in molecular docking analysis, the best docking score was displayed by the most active compound  3d supported the in vitro inhibition results. Compound 3d emerged to be promising lead for the further development of anti- Alzheimer’s drugs.

Keywords

Alzheimer’s disease AChE inhibition Aminothiazole Antioxidant Molecular docking
Soni, A., Kumar, A., Kumar, V., Rawat, R., & Eyupoglu, V. (2024). Synthesis and Evaluation of Aminothiazole Hybrids as Potential Acetylcholinesterase Inhibitors. Asian Journal of Chemistry, 36(5), 1126–1134. https://doi.org/10.14233/ajchem.2024.31241
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
References
  1. R. Sengoku, Neuropathology, 40, 22 (2020); https://doi.org/10.1111/neup.12626
  2. P.S. Aisen and K.L. Davis, Neurology, 48(5suppl_6), 35S (1997); https://doi.org/10.1212/WNL.48.5_Suppl_6.35S
  3. R. Hussain, H. Ullah, F. Rahim, M. Sarfraz, M. Taha, R. Iqbal, W. Rehman, S. Khan, S.A.A. Shah, S. Hyder, M. Alhomrani, A.S. Alamri, O. Abdulaziz and M.A. Abdelaziz, Molecules, 27, 6087 (2022); https://doi.org/10.3390/molecules27186087
  4. M.S. Uddin, A. Al Mamun, M.T. Kabir, M. Jakaria, B. Mathew, G.E. Barreto and G.M. Ashraf, Mol. Neurobiol., 56, 4925 (2019); https://doi.org/10.1007/s12035-018-1420-2
  5. https://www.who.int/news-room/fact-sheets/detail/dementia
  6. R.-M. Lu, Y.-C. Hwang, I.-J. Liu, C.-C. Lee, H.-Z. Tsai, H.-J. Li and H.-C. Wu, J. Biomed. Sci., 27, 1 (2020); https://doi.org/10.1186/s12929-019-0592-z
  7. S.P. Yun, D. Kim, S. Kim, S.M. Kim, S.S. Karuppagounder, S.-H. Kwon, S. Lee, T.-I. Kam, S. Lee, S. Ham, J.H. Park, V.L. Dawson, T.M. Dawson, Y. Lee and H.S. Ko, Mol. Neurodegener., 13, 1 (2018); https://doi.org/10.1186/s13024-017-0233-5
  8. B.L. Sun, W.W. Li, C. Zhu, W.-S. Jin, F. Zeng, Y.-H. Liu, X.-L. Bu, J. Zhu, X.-Q. Yao and Y.-J. Wang, Neurosci. Bull., 34, 1111 (2018); https://doi.org/10.1007/s12264-018-0249-z
  9. S.E. Swalley, Bioorg. Med. Chem., 28, 115239 (2020); https://doi.org/10.1016/j.bmc.2019.115239
  10. J. Fang, Y. Li, R. Liu, X. Pang, C. Li, R. Yang, Y. He, W. Lian, A.-L. Liu and G.-H. Du, J. Chem. Inf. Model., 55, 149 (2015); https://doi.org/10.1021/ci500574n
  11. P. Zhang, S. Xu, Z. Zhu and Z. Xu, Eur. J. Med. Chem., 176, 228 (2019); https://doi.org/10.1016/j.ejmech.2019.05.020
  12. S.-Y. Hung and W.-M. Fu, J. Biomed. Sci., 24, 47 (2017); https://doi.org/10.1186/s12929-017-0355-7
  13. C. Ballard, S. Gauthier, A. Corbett, C. Brayne, D. Aarsland and E. Jones, Lancet, 377, 1019 (2011); https://doi.org/10.1016/S0140-6736(10)61349-9
  14. G. Marucci, M. Buccioni, D.D. Ben, C. Lambertucci, R. Volpini and F. Amenta, Neuropharmacology, 190, 108352 (2021); https://doi.org/10.1016/j.neuropharm.2020.108352
  15. Y. Zhao and B. Zhao, Oxid. Med. Cell. Longev., 2013, 316523 (2013); https://doi.org/10.1155/2013/316523
  16. M.T. Islam, Neurol. Res., 39, 73 (2017); https://doi.org/10.1080/01616412.2016.1251711
  17. M. Gubandru, D. Margina, C. Tsitsimpikou, N. Goutzourelas, K. Tsarouhas, M. Ilie, A.M. Tsatsakis and D. Kouretas, Food Chem. Toxicol., 61, 209 (2013); https://doi.org/10.1016/j.fct.2013.07.013
  18. D.J. Hardy and D.J. Selkoe, Science, 297, 353 (2002); https://doi.org/10.1126/science.1072994
  19. B.N. Saglik, D. Osmaniye, U.A. Çevik, S. Levent, B.K. Çavusoglu, Y. Özkay and Z.A. Kaplancikli, Molecules, 25, 4312 (2020); https://doi.org/10.3390/molecules25184312
  20. B. Kilic, M. Bardakkaya, R. Ilikci Sagkan, F. Aksakal, S. Shakila and D.S. Dogruer, Bioorg. Chem., 131, 106322 (2023); https://doi.org/10.1016/j.bioorg.2022.106322
  21. H.A. Ghabbour, A.A. Kadi, K.E. ElTahir, R.F. Angawi and H.I. ElSubbagh, Med. Chem. Res., 24, 3194 (2015); https://doi.org/10.1007/s00044-015-1371-3
  22. E.O. Al-Tamimi and H.F. Abdul Mahdi, Int. J. Curr. Microbiol. Appl. Sci., 5, 1 (2016); https://doi.org/10.20546/ijcmas.2016.508.001
  23. K. Rehse and T. Baselt, Arch. Pharm. (Weinheim), 341, 645 (2008); https://doi.org/10.1002/ardp.200700046
  24. A.M. Mohamed, N.A. Abdel-Hafez, A.F. Kassem, E.M.H. Abbas and M.M. Mounier, Russ. J. Gen. Chem., 87, 2391 (2017); https://doi.org/10.1134/S1070363217100218
  25. C.I. Lino, I. Gonçalves de Souza, B.M. Borelli, T.T. Silvério-Matos, I.N. Santos Teixeira, J.P. Ramos, E. Maria de Souza Fagundes, P. de Oliveira Fernandes, V.G. Maltarollo, S. Johann and R.B. de Oliveira, Eur. J. Med. Chem., 151, 248 (2018); https://doi.org/10.1016/j.ejmech.2018.03.083
  26. J.A. Kaplancikli, G. Turan-Zitouni, G. Revial and K. Guven, Arch. Pharm. Res., 27, 1081 (2004); https://doi.org/10.1007/BF02975108
  27. M. Modriæ, M. Bozicevic, I. Faraho, M. Bosnar and I. Skoric, J. Mol. Struct., 1239, 130526 (2021); https://doi.org/10.1016/j.molstruc.2021.130526
  28. I.N. Korkmaz, Biotechnol. Appl. Biochem., 70, 659 (2023); https://doi.org/10.1002/bab.2388
  29. P. Arora, R. Narang, S.K. Nayak, S.K. Singh and V. Judge, Med. Chem. Res., 25, 1717 (2016); https://doi.org/10.1007/s00044-016-1610-2
  30. C.B. Mishra, S. Kumari and M. Tiwari, Eur. J. Med. Chem., 92, 1 (2015); https://doi.org/10.1016/j.ejmech.2014.12.031
  31. M.F. Arshad, A. Alam, A.A. Alshammari, M.B. Alhazza, I.M. Alzimam, M.A. Alam, G. Mustafa, M.S. Ansari, A.M. Alotaibi, A.A. Alotaibi, S. Kumar, S.M.B. Asdaq, M. Imran, P.K. Deb, K.N. Venugopala and S. Jomah, Molecules, 27, 3994 (2022); https://doi.org/10.3390/molecules27133994
  32. N.H. Elghazawy, D. Zaafar, R.R. Hassan, M.Y. Mahmoud, L. Bedda, A.F. Bakr and R.K. Arafa, ACS Chem. Neurosci., 13, 1187 (2022); https://doi.org/10.1021/acschemneuro.1c00766
  33. B.F.D. Gatphoh, N.N. Aggarwal, H. Kumar and B.C. Revanasiddappa, Thai J. Pharm. Sci., 45, 492 (2021).
  34. G. Sahin, E. Palaska, M. Ekizoglu and M. Özalp, Il Farmaco, 57, 539 (2002); https://doi.org/10.1016/S0014-827X(02)01245-4
  35. S.S. Thakkar, P. Thakor, H. Doshi and A. Ray, Bioorg. Med. Chem., 25, 4064 (2017); https://doi.org/10.1016/j.bmc.2017.05.054
  36. M.A. Tantray, I. Khan, H. Hamid, M.S. Alam, A. Dhulap and A. Kalam, Bioorg. Chem., 77, 393 (2018); https://doi.org/10.1016/j.bioorg.2018.01.040
  37. A.G. Banerjee, N. Das, S.A. Shengule, R.S. Srivastava and S.K. Shrivastava, Eur. J. Med. Chem., 101, 81 (2015); https://doi.org/10.1016/j.ejmech.2015.06.020
  38. B. Yadagiri, S. Gurrala, R. Bantu, L. Nagarapu, S. Polepalli, G. Srujana and N. Jain, Bioorg. Med. Chem. Lett., 25, 2220 (2015); https://doi.org/10.1016/j.bmcl.2015.03.032
  39. W. Wu, Q. Chen, A. Tai, G. Jiang and G. Ouyang, Bioorg. Med. Chem. Lett., 25, 2243 (2015); https://doi.org/10.1016/j.bmcl.2015.02.069
  40. P. Mishra, P. Sharma, P.N. Tripathi, S.K. Gupta, P. Srivastava, A. Seth, A. Tripathi, S. Krishnamurthy and S.K. Shrivastava, Bioorg. Chem., 89, 103025 (2019); https://doi.org/10.1016/j.bioorg.2019.103025
  41. A. Soni, A. Kumar, V. Kumar, R. Rawat and V. Eyupoglu, Future Med. Chem., 16, 513 (2024); https://doi.org/10.4155/fmc-2023-0290
  42. N. Singh, U.S. Sharma, N. Sutar, S. Kumar and U.K. Sharma, J. Chem. Pharm. Res., 2, 691 (2010).
  43. H. Bayrak, A. Demirbas, N. Demirbas and S.A. Karaoglu, Eur. J. Med. Chem., 44, 4362 (2009); https://doi.org/10.1016/j.ejmech.2009.05.022
  44. E. Garibov, P. Taslimi, A. Sujayev, Z. Bingol, S. Çetinkaya, I. Gulçin, S. Beydemir, V. Farzaliyev, S.H. Alwasel and C.T. Supuran, J. Enzyme Inhib. Med. Chem., 31(sup3), 1 (2016); https://doi.org/10.1080/14756366.2016.1198901
  45. L.M. Magalhães, M.A. Segundo, S. Reis and J.L.F.C. Lima, Anal. Chim. Acta, 613, 1 (2008); https://doi.org/10.1016/j.aca.2008.02.047
  46. M. Elmastas, I. Gülcin, S. Beydemir, Ö. Irfan Küfrevioglu and H.Y. Aboul-Enein, Anal. Lett., 39, 47 (2006); https://doi.org/10.1080/00032710500423385
  47. Schrödinger Suite Release, 2018-3: Glide. New York, NY, Schrödinger, LLC (2018).
  48. R.A. Friesner, R.B. Murphy, M.P. Repasky, L.L. Frye, J.R. Greenwood, T.A. Halgren, P.C. Sanschagrin and D.T. Mainz, J. Med. Chem., 49, 6177 (2006); https://doi.org/10.1021/jm051256o
  49. H. Bekker, H.J.C. Berendsen, E.J. Dijkstra, S. Achterop, R. Vondrumen, D. Vanderspoel, A. Sijbers, H. Keegstra and M.K.R. Renardus, GROMACS-A Parallel Computer for Molecular-Dynamics Simulations, In 4th International Conference on Computational Physics, World Scientific Publishing, Singapore, pp. 252-256 (1993).
  50. A. Ganesan, M.L. Coote and K. Barakat, Drug Discov. Today, 22, 249 (2017); https://doi.org/10.1016/j.drudis.2016.11.001
  51. N. Schmid, A.P. Eichenberger, A. Choutko, S. Riniker, M. Winger, A.E. Mark and W.F. van Gunsteren, Eur. Biophys. J., 40, 843 (2011); https://doi.org/10.1007/s00249-011-0700-9
  52. P. Mark and L. Nilsson, J. Phys. Chem. A, 105, 9954 (2001); https://doi.org/10.1021/jp003020w
  53. W.F. Van Gunsteren and H.J.C. Berendsen, Mol. Simul., 1, 173 (1988); https://doi.org/10.1080/08927028808080941
  54. H.J.C. Berendsen, D. van der Spoel and R. van Drunen, Comput. Phys. Commun., 91, 43 (1995); https://doi.org/10.1016/0010-4655(95)00042-E
  55. B. Hess, H. Bekker, H.J.C. Berendsen and J.G.E.M. Fraaije, J. Comput. Chem., 18, 1463 (1997); https://doi.org/10.1002/(SICI)1096-987X(199709)18:12<1463::AIDJCC4>3.0.CO;2-H
  56. M. Di Pierro, R. Elber and B. Leimkuhler, J. Chem. Theory Comput., 11, 5624 (2015); https://doi.org/10.1021/acs.jctc.5b00648
  57. W. Humphrey, A. Dalke and K. Schulten, J. Mol. Graph., 14, 33 (1996); https://doi.org/10.1016/0263-7855(96)00018-5
  58. R. Rawat, K. Kant, A. Kumar, K. Bhati and S.M. Verma, Future Med. Chem., 13, 447 (2021); https://doi.org/10.4155/fmc-2020-0191
  59. A. Vaught and J. Linux (1996); www.linuxjournal.com/article/1218
Read More
Author biographies is not available.
Statistic
Read Counter : 0 Download : 0