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In Silico Studies and DNA Cleavage, Antioxidant, Acetylcholinesterase, and Butyrylcholinesterase Activity Evaluation of Bis-Histamine Schiff Bases and Bis-Spinaceamine Substituted Derivatives

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Pharmaceutical Chemistry Journal Aims and scope

In this work, a series of seven bis-histamine Schiff bases (H1–H4) and bis-spinaceamine substituted derivatives (SPH1, SPH2, and SPH4) were successfully re-synthesized to evaluate their antioxidant properties by several bioanalytical methods such as DPPH free radical scavenging assay, ABTS radical cation decolorization assay, metal chelating and CUPRAC methods. On the other hand, these compounds were also investigated as inhibitors of acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and DNAcleavage. The results revealed that all compounds showed, in general, moderate DPPH and ABTS radical scavenging activities, and low metal chelating and CUPRAC activities. Specifically, compound SPH4 showed good DPPH radical scavenging activity with IC50 value of 59.59 μM, which is better than the BHA and BHT standard values. The best AChE and BChE inhibition results among the tested series were also obtained for compound SPH4 with % inhibition values of 84.51 and 75.89, respectively. Taken together, compound SPH4 might be an interesting lead compound to discover more potent agents against these enzymes.

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References

  1. N. Lolak, M. Boga, M. Tuneg, et al., J. Enzyme Inhib. Med. Chem., 35(1), 424 – 431 (2020).

    Article  CAS  Google Scholar 

  2. I. Zueva, J. Dias, S. Lushchekina, et al., Neuropharmacology, 155, 131 – 141 (2019).

    Article  CAS  Google Scholar 

  3. P. Taslimi, M. Işık, F. Türkan, et al., J. Biomol. Struct. Dyn., (2020). https: //doi.org/https://doi.org/10.1080/07391102.2020.1790422.

  4. N. Lolak, S. Akocak, C. Turkeş, et al., Bioorg. Chem., 100, 103897 (2020).

    Article  CAS  Google Scholar 

  5. D. O. Ozgun, H. I. Gul, C. Yamali, et al., Bioorg. Chem., 84, 511 – 517 (2019).

    Article  Google Scholar 

  6. S. V. Lushchekina and P. Masson, Neuropharmacology, 177, 108236 (2020).

    Article  CAS  Google Scholar 

  7. S. Akocak, N. Lolak, A. Nocentini, et al., Bioorg. Med. Chem., 25, 3093 – 3097 (2017).

    Article  CAS  Google Scholar 

  8. S. Akocak, M. R. Alam, A. M. Shabana, et al., J. Med. Chem., 59(10), 5077 – 5088 (2016).

    Article  CAS  Google Scholar 

  9. M. Abellán-Flos, M. Tanç, C. T. Supuran, et al., J. Enzyme Inhib. Med. Chem., 31(6), 946 – 52 (2016).

    Article  Google Scholar 

  10. M. Abellán-Flos, M. Tanç, C. T. Supuran, and S. P. Vincent, Org. Biomol. Chem., 13(27), 7445 – 7451 (2015).

    Article  Google Scholar 

  11. B. Draghici, D. Vullo, S. Akocak, et al., Chem. Commun (Camb.), 50(45), 5980 – 5983 (2014).

    Article  CAS  Google Scholar 

  12. S. Akocak, N. Lolak, S. Bua, et al., J. Enzyme Inhib. Med. Chem., 34(1), 1193 – 1198 (2019).

    Article  CAS  Google Scholar 

  13. M. S. Blois, Nature, 181, 1199 – 1200 (1958)

    Article  CAS  Google Scholar 

  14. S. Akocak, N. Lolak, M. Tuneg, and M. Boga, J. Turk. Chem. Soc. Sec. A: Chem., 6(2), 157 – 164 (2019).

    Article  CAS  Google Scholar 

  15. N. Lolak and S. Akocak, Cumhuriyet Sci. J., 41(2), 413 – 418 (2020).

    Article  Google Scholar 

  16. R. Re, N. Pellegrini, A. Proteggente, et al., Free Radic. Biol. Med., 26(9–10), 1231 – 1237 (1999).

    Article  CAS  Google Scholar 

  17. S. Akocak, M. Boga, N. Lolak, et al., J. Turk. Chem. Soc. Sec. A: Chem., 6(1), 63 – 70 (2019).

    Article  CAS  Google Scholar 

  18. M. Oguz, E. Kalay, S. Akocak, et al., J. Enzyme Inhib. Med. Chem., 35(1), 1215 – 1223 (2020).

    Article  CAS  Google Scholar 

  19. T. C. Dinis, V. M. Madeira and L. M. Almeida, Arch. Biochem. Biophys., 315(1), 161 – 170 (1994).

    Article  CAS  Google Scholar 

  20. N. Lolak, M. Tuneg, A. Doğan, et al., Bioorg. Med. Chem. Rep., 3(2), 22 – 31 (2020).

    Article  Google Scholar 

  21. G. L. Ellman, K. D. Courtney, V. Andres, and R. M. Featherstone, Biochem. Pharmacol., 7, 88 – 95 (1961).

    Article  CAS  Google Scholar 

  22. O. Gerlits, K. Y. Ho, X. Cheng, et al., Chem. Biol. Interact., 309, 108698 (2019).

    Article  CAS  Google Scholar 

  23. A. Meden, D. Knez, M. Jukiè, et al., Chem. Commun. (Camb.), 55(26), 3765 – 3768 (2019).

    Article  CAS  Google Scholar 

  24. M. Iþýk, S. Akocak, N. Lolak, et al., Archiv der Pharmazie, 353(9), 2000102 (2020).

    Article  Google Scholar 

  25. M. Durgun, C. Türkeş, M. Işık, et al., J. Enzyme Inhib. Med. Chem., 35(1), 950 – 962 (2020).

    Article  CAS  Google Scholar 

  26. M. Işık, Y. Demir, M. Durgun, et al., Chem. Papers, 74, 1395 – 1405 (2020).

    Article  Google Scholar 

  27. M. Bingul, S. Ercan and M. Boga, J. Mol. Struct., 1213, 128202 (2020).

    Article  CAS  Google Scholar 

  28. P. R. Reddy and P. Manjula, Chem. Biodiver., 4(3), 468 – 480 (2007).

    Article  CAS  Google Scholar 

  29. S. I. Kirin, C. M. Happel, S. Hrubanova, et al., Dalton Trans., 21(8), 1201 – 1207 (2004).

    Article  Google Scholar 

  30. S. 30. S. Massoud, F. R. Louka, W. Xu, et al., Eur. J. Inorg. Chem., 2011(23), 3469 – 3479 (2011).

  31. U. Chaveerach, A. Meenongwa, Y. Trongpanich, et al., Polyhedron, 29(2), 731 – 738 (2010).

    Article  CAS  Google Scholar 

  32. S. S. Tonde, A. S. Kumbhar, S. B. Padhye, and R. J. Butcher; J. Inorg. Biochem., 100(1), 51 – 57 (2006).

    Article  CAS  Google Scholar 

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Acknowledgements

This work was partially supported by The Scientific and Technological Research Council of Turkey (TUBITAK), Research Fund Project No. 215Z484.

CONFLICT OF INTEREST

The authors declare that they have no conflicts of interest.

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Authors and Affiliations

  1. Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Adiyaman University, 02040, Adiyaman, Turkey

    Nebih Lolak, Aslinur Dogan & Suleyman Akocak

  2. Department of Analytical Chemistry, Faculty of Pharmacy, Dicle University, 21280, Diyarbakir, Turkey

    Mehmet Boga & Muhammed Tuneg

  3. Department of Pharmaceutical Botany, Faculty of Pharmacy, Adiyaman University, 02040, Adiyaman, Turkey

    Gorkem Deniz Sonmez

Authors
  1. Nebih Lolak
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  2. Mehmet Boga
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  3. Gorkem Deniz Sonmez
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  4. Muhammed Tuneg
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  5. Aslinur Dogan
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  6. Suleyman Akocak
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Correspondence to Suleyman Akocak.

Additional information

Translated from Khimiko-Farmatsevticheskii Zhurnal, Vol. 56, No. 1, pp. 10 – 10, January, 2022.

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Lolak, N., Boga, M., Sonmez, G.D. et al. In Silico Studies and DNA Cleavage, Antioxidant, Acetylcholinesterase, and Butyrylcholinesterase Activity Evaluation of Bis-Histamine Schiff Bases and Bis-Spinaceamine Substituted Derivatives. Pharm Chem J 55, 1338–1344 (2022). https://doi.org/10.1007/s11094-022-02581-7

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  • DOI: https://doi.org/10.1007/s11094-022-02581-7

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