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Journals / International Journal of Chemistry and Technology / 2026 / Volume: 8 Issue: 1

Synthesis, Biological Activity Studies and Molecular Modeling Studies of Chalcone Compounds with Methyl Group

Bedriye Seda Kurşun Aktar(MALATYA TURGUT ÖZAL ÜNİVERSİTESİ YEŞİLYURT MESLEK YÜKSEKOKULU)0000-0002-1492-3266
Pages
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Publication Date
2024-06-05
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

According to molecular docking results, all molecules were found to be more active than the reference compounds.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:A series of new chalcone derivatives (1-5) were synthesized as a result of the Claisen-Schmidt condensation of different substituted methyl aldehydes of 4′-Piperazinoacetophenone.
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Key Findings & Data:While compound 1 is the most active molecule in AChE (IC50= 16.29±0.44 μM), BChE (IC50 = 10.19±0.04 μM) and α-amylase (IC50= 105.51±0.24 μM) inhibitor activities; Compound 5 was found to be the most active molecule in α-glucosidase inhibitor activity.
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Conclusion & Impact:According to molecular docking results, all molecules were found to be more active than the reference compounds.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Chalcone · anticholinesterase inhibitory · α-amylase inhibitory

Abstract

A series of new chalcone derivatives (1-5) were synthesized as a result of the Claisen-Schmidt condensation of different substituted methyl aldehydes of 4′-Piperazinoacetophenone. Anticholinesterase (AChE and BChE) inhibitory activity and antidiabetic (α-glucosidase and α-amylase inhibitory) activities of the synthesized compounds were examined. While compound 1 is the most active molecule in AChE (IC50= 16.29±0.44 μM), BChE (IC50 = 10.19±0.04 μM) and α-amylase (IC50= 105.51±0.24 μM) inhibitor activities; Compound 5 was found to be the most active molecule in α-glucosidase inhibitor activity. In silico and molecular docking studies of compounds 1-5 were performed. According to molecular docking results, all molecules were found to be more active than the reference compounds.

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Cite This Article

Aktar, B. S. K. (2024). Synthesis, Biological Activity Studies and Molecular Modeling Studies of Chalcone Compounds with Methyl Group. International Journal of Chemistry and Technology, Volume: 8 Issue: 1. https://doi.org/10.32571/ijct.1389889

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References (37)

  1. Ha, M.T.; Seong, S.H.; Nguyen, T.D.; Cho, W.K.; Ah, K.J.; Mae, J.Y.; Woo, M.H.; Choi, J.S.; Min, B.S. Phytochemistry. 2018, 155, 114–125.
  2. Aktar, B.S.K.; Sıcak, Y.; Tok, T.T.; Emre, O.E.E.; Yağlıoğlu, A.Ş.; Iyidoğan, A.K.; Demirtaş, I. J. Mol. Struct. 2020,1211, 128059.
  3. Chen, M.; Christensen, S.B.; Blom, J.; Lemmich, E.; Nadelmann, L.; Fich, K.; Kharazmi, A. Antimicrob. Agents Chemother. 1993, 37(12), 2550-2556.
  4. Birari, R.B.; Gupta, S.; Mohan, C.G.; Bhutani, K.K. Phytomedicine. 2011, 18(8-9), 795-801.
  5. Aktar, B.S.K.; Sıcak, Y.; Emre, O.E.E. Int. J. Chem. Technol. 2022, 6(1), 7-14.
  6. Tomar, V.; Bhattacharjee, G.; Rajakumar, S.; Srivastava, K.; Puri, S. K. Eur. J. Med. Chem. 2010, 45(2), 745-751.
  7. Sashidhara, K.V.; Palnati, G.R.; Sonkar, R.; Avula, S.R.; Awasthi, C.; Bhatia, G. Eur. J. Med. Chem. 2013, 64, 422-431.
  8. Wang, J.; Wang, N.; Yao, X.; Kitanaka, S.亚洲传统医药, 2007, 2(1), 23-29.
  9. Rizvi, S.U.F.; Siddiqui, H.L.; Johns, M.; Detorio, M.; Schinazi, R.F. 2012. Med. Chem. Res. 21, 3741-3749.
  10. Israf, D.A.; Khaizurin, T.A.; Syahida, A.; Lajis, N.H.; Khozirah, S. Mol. Immunol. 2007, 44(5), 673-679.
  11. Lee, Y.S.; Lim, S.S.; Shin, K.H.; Kim, Y.S.; Ohuchi, K.; Jung, S.H. Biol. Pharm. Bull. 2006, 29(5), 1028-1031.
  12. Kim, D.W.; Curtis-Long, M.J.; Yuk, H.J.; Wang, Y.; Song, Y.H.; Jeong, S.H.; Park, K.H. Food chemistry. 2014,153, 20-27. 13. Abdullah, M.I.; Mahmood, A.; Madni, M.; Masood, S.; Kashif, M. Bioorg. Chem. 2014, 54, 31-37.
  13. Mahapatra, D.K.; Asati, V.; Bharti, S.K. 2015, Eur. J. Med. Chem. 92, 839-865.
  14. Cho, S.; Kim, S.; Jin, Z.; Yang, H.; Han, D.; Baek, N.I.; Jin, Y.H. Biochemical and Biochem. Biophys. Res. Commun. 2011, 413(4), 637-642.
  15. Alsayed, S.S.; Beh, C.C.; Foster, N.R.; Payne, A.D.; Yu, Y.; Gunosewoyo, H. Current Mol. Pharmacol. 2019, 12(1), 27-49.
  16. Jamal, H.; Ansari, W.H.; Rizvi, S.J. Fund. Clin. Pharmacol. 2008, 22(6), 673-681.
  17. Kursun Aktar, B.S.; Oruç-Emre, E.E.; Demirtas¸ I., Sahin Yaglioglu, A.; Guler, C.; Adem, S.; Karaküçük Iyidogan, A. J. Mol. Struct. 2017, 1149, 632-639.
  18. Ranjit, P.M.; Rahaman, S.A.; Kumar, K.P.; Prasad, Y.R.; Santhipriya, T.; Manikanta, G.C. V.S.; Sudeepthi, N.R.L. Int. J. PharmTech Res, 2013,5(1), 284-293.
  19. Ellman, G.L.; Courtney, K.D.; Andres, V.; Featherston, R.M. Biochem. Pharmacol. 1961, 7, 88-95.
  20. Quan, N.; Xuan, T.; Tran, H.D.; Thuy, N.; Trang, L.; Huong, C.; Tuyen, P. Molecules. 2019, 24(3), 605.
  21. Kim, J.S.; Kwon, C.S.; Son, K.H. Biosci. Biotechnol. Biochem. 2000, 64(11), 2458-2461.
  22. Adme Daina, A.; Michielin, O.; Zoete, V. Sci. Rep. 2017, 7(1), 42717.
  23. Mol Molsoft molecules in silico. http://molsoft.com/ mprop (Accessed September 9, 2023)
  24. Organic Chemistry Portal. https://www.organic-chemistry.org/ (Accessed on 20 May 2023).
  25. Morris, G.M.; Huey, R.; Lindstrom, W.; Sanner, M.F.; Belw, R.K.; Goodsell, D.S.; Olson, A.J. J. Comput. Chem. 2009, 30(16), 2785-2791.
  26. Sıcak, Y.; Kekeçmuhammed, H.; Karaküçük‐İyidoğan, A.; Taşkın‐Tok, T.; Oruç‐Emre, E. E.; Öztürk, M. J. Mol. Recognit. 2023, e3020.
  27. Aktar, B. S. K. Russ. J. Bioorg. Chem. 2023, 49(5), 1023-1033.
  28. Kurşun‐Aktar, B.S.; Adem, Ş.; Tatar‐Yilmaz, G.; Hameed, Z.A.H.; Oruç‐Emre, E.E. J. Mol. Recognit, 2023, e3061.
  29. Sıcak, Y. Med. Chem. Res. 2021, 30(8), 1557-1568.
  30. Sıcak, Y. Turk J Chem. 2021, DOI: 10.3906/kim-2107-27.
  31. Barak, D.; Kronman, C.; Ordentlich, A.; Ariel, N.; Bromberg, A.; Marcus, D; Shafferman, A. J. Biol. Chem. 1994, 269(9), 6296-6305.
  32. Quinn, D.M. Chemical reviews. 1987,87(5), 955-979.
  33. Masson, P.; Legrand, P.; Bartels, C.F.; Froment, M.T.; Schopfer, L.M.; Lockridge, O. Biochemistry. 1997,36(8), 2266-2277.
  34. Nachon, F.; Ehret-Sabatier, L.; Loew, D.; Colas, C.; van Dorsselaer, A.; Goeldner, M. Biochemistry. 1998, 37(29), 10507-10513.
  35. Williams, L.K.; Zhang, X.; Caner, S.; Tysoe, C.; Nguyen, N.T.; Wicki, J.; Brayer, G.D. The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif. Nat. Chem. Biol. 2015, 11(9), 691-696.
  36. Roig-Zamboni, V.; Cobucci-Ponzano, B.; Iacono, R.; Ferrara, M. C.; Germany, S.; Bourne, Y.; Sulzenbacher, G. Nat. Commun, 2017, 8(1), 1111.
  37. Williams, L.K.; Zhang, X.; Caner, S.; Tysoe, C.; Nguyen, N.T.; Wicki, J.; Brayer, G.D. 2015. Nat. Chem. Biol. 11(9), 691-696