European Journal of Chemistry

Synthesis, and evaluation of α-amylase and α-glucosidase inhibitory potential of new pyrazolo[3,4-d]pyrimidine derivatives

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Published: Jun 30, 2017
DOI: https://doi.org/10.5155/eurjchem.8.2.105-108.1541
Keywords:
α-Amylase, IC50 values, α-Glucosidase, Inhibitory activity, 1, 3-Dipolarcyclo addition, Pyrazolo[3, 4-d]pyrimidine
Section
Research Article
Issue
Vol. 8 No. 2 (2017): June 2017
Dates
Received 2016-12-31
Accepted 2017-01-07
Published 2017-06-30


Main Article Content

Mohammed El-Fal
Medicinal Chemistry Laboratory, Faculty of Medicine and Pharmacy, Mohammed V University, 10170, Rabat, Morocco
Karima Sayah
Laboratories of Pharmacology and Toxicology, Faculty of Medicine and Pharmacy, Mohammed V University, 10170, Rabat, Morocco
Ilias Marmouzi
Laboratories of Pharmacology and Toxicology, Faculty of Medicine and Pharmacy, Mohammed V University, 10170, Rabat, Morocco
My El Abbes Faouzi
Laboratories of Pharmacology and Toxicology, Faculty of Medicine and Pharmacy, Mohammed V University, 10170, Rabat, Morocco
M'hammed Ansar
Medicinal Chemistry Laboratory, Faculty of Medicine and Pharmacy, Mohammed V University, 10170, Rabat, Morocco
Jamal Taoufik
Medicinal Chemistry Laboratory, Faculty of Medicine and Pharmacy, Mohammed V University, 10170, Rabat, Morocco
El Mokhtar Essassi
Laboratory of Organic Heterocyclic Chemistry URAC 21, Faculty of Sciences, Mohammed V University, 10170, Rabat, Morocco
Youssef Ramli
Medicinal Chemistry Laboratory, Faculty of Medicine and Pharmacy, Mohammed V University, 10170, Rabat, Morocco

Abstract

A series of new pyrazolo[3,4-d]pyrimidine compounds were synthesized in excellent yields via sulfuration and 1,3-dipolar cycloaddition and confirmed by MS, FT-IR and NMR techniques. All the prepared compounds were screened in vitro for their α-amylase and α-glucosidase inhibitory activities. Preliminary results indicated that some target compounds exhibited promising α-amylase and α-glucosidase inhibitory activity potency. Among the tested products, the cycloadduct f was found most active inhibitor (IC50 = 134.30 μM) for α-amylase, and the sulphur product b is the most active inhibitor (IC50 = 16.37 μM) for α-glucosidase.


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El-Fal, M.; Sayah, K.; Marmouzi, I.; Faouzi, M. E. A.; Ansar, M.; Taoufik, J.; Essassi, E. M.; Ramli, Y. Synthesis, and Evaluation of α-Amylase and α-Glucosidase Inhibitory Potential of New pyrazolo[3,4-d]pyrimidine Derivatives. Eur. J. Chem. 2017, 8, 105-108.

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References

[1]. IDF Diabetes Atlas. Brussels, Belgium: International Diabetes Federation, 7th ed. 2015, http://www.diabetesatlas.org

[2]. Rossi, E. J.; Sim, L.; Kuntz, D. A.; Hahn, D.; Johnston, B. D.; Ghavami, A.; Rose, D. R. Fed. Eur. Biochem. Soc. J. 2006, 273, 2673-2683.

[3]. Matthews, D. R.; Hosker, J. P.; Rudenski, A. S.; Naylor, B. A.; Treacher, D. F.; Turner, R. C. Diabetologia. 1985, 28, 412-419.
https://doi.org/10.1007/BF00280883

[4]. Kawahito, S.; Kitahata, H.; Oshita, S. World J. Gastroentero. 2009, 15, 4137-4142.
https://doi.org/10.3748/wjg.15.4137

[5]. Saltos, M. B. V.; Puente, B. F. N.; Faraone, I.; Milella, L.; De Tommasi, N.; Braca, A. Phytochem. Lett. 2015, 14, 45-50.
https://doi.org/10.1016/j.phytol.2015.08.018

[6]. Kim, J. S.; Kwon, C. S.; Son, K. H. Biosci. Biotech. Bioch. 2000, 64, 2458-2461.
https://doi.org/10.1271/bbb.64.2458

[7]. Kwon, Y. I.; Apostolidis, E.; Shetty, K. J. Food Biochem. 2007, 31, 370-385.
https://doi.org/10.1111/j.1745-4514.2007.00120.x

[8]. Hano, C.; Renouard, S.; Molinie, R. Bioorg. Med. Chem. Lett. 2013, 23, 3007-3012.
https://doi.org/10.1016/j.bmcl.2013.03.029

[9]. Ramadhan, R.; Phuwapraisirisan, P. Bioorg. Med. Chem. Lett. 2015, 25, 2529-2533.
https://doi.org/10.1016/j.bmcl.2015.08.069

[10]. Mahmoud, H. I.; El-Rab, S. M. G. B, Khalil, A. F.; Ismael, S. M. Eur. J. Chem. 2014, 5, 65‐72.
https://doi.org/10.5155/eurjchem.5.1.65-72.903

[11]. Taher, M. A. H.; Dawood, D. H.; Sanad, M. I.; Hassan, R. A. Eur. J. Chem. 2016, 7, 397‐404.
https://doi.org/10.5155/eurjchem.7.4.397-404.1478

[12]. McInnes, G. T.; Lawson, D. H.; Jick, H. Ann. Rheum. Dis. 1981, 40, 245-249.
https://doi.org/10.1136/ard.40.3.245

[13]. Gruchalla, R. S.; J. Allergy Clin. Immunol. 2003, 111, 548-559.
https://doi.org/10.1067/mai.2003.93

[14]. Zimmerman, H. J.; Maddrey, W. C. Hepatology 1995, 22, 767-773.
https://doi.org/10.1002/hep.1840220312

[15]. Horsmans, Y. Gastroenterol Clin. Biol. 1993, 17, 25-30.
https://doi.org/10.1097/00004836-199307000-00008

[16]. El Fal, M.; Ramli, Y.; Essassi, E. M.; Saadi, M.; El Ammari, L. Acta Cryst. E 2014, 70, o1005-o1006.
https://doi.org/10.1107/S160053681401825X

[17]. El Fal, M.; Ramli, Y.; Essassi, E. M.; Saadi, M.; El Ammari, L. Acta Cryst. E 2014, 70, o1038-o1038.
https://doi.org/10.1107/S1600536814018042

[18]. El Fal, M.; Ramli, Y.; Essassi, E. M.; Saadi, M.; El Ammari, L. Acta Cryst. E 2013, 69, o1650-o1650.
https://doi.org/10.1107/S160053681302789X

[19]. El Fal, M.; Ramli, Y.; Essassi, E. M.; Saadi, M.; El Ammari, L. Acta Cryst. E 2015, 71, o95-o96.
https://doi.org/10.1107/S2052520615000864

[20]. Alsubari, A.; Ramli, Y.; Essassi, E. M.; Zouihri, H. Acta Cryst. E 2011, 67, o1926-o1926.
https://doi.org/10.1107/S1600536811025025

[21]. El Fal, M.; Ramli, Y.; Essassi, E. M.; Saadi, M.; El Ammari, L. Acta Cryst. E 2015, 71, o769-o770.

[22]. El Fal M.; Ramli, Y.; Essassi, E. M.; Saadi, M.; El Ammari, L. Acta Cryst. E 2014, 70, o1281-o1281.
https://doi.org/10.1107/S1600536814025239

[23]. El Fal, M.; Ramli, Y.; Zerzouf, A.; Talbaoui, A.; Bakri, Y.; Essassi, E. M. J. Chem. 2015, Article ID 982404, http://dx.doi.org/10.1155/2015/982404
https://doi.org/10.1155/2015/982404

[24]. Sayah, K.; Marmouzi, I.; NaceiriMrabti, H.; Cherrah, Y.; Faouzi, M. E. A. Biomed. Res. Int. 2017, 7, ID 2789482, http://dx.doi.org/10.1155/2017/2789482
https://doi.org/10.1155/2017/2789482

[25]. Bhandari, M. R.; Jong-Anurakkun, N.; Hong, G.; Kawabata, J. Food Chem. 2008, 106, 247-252.
https://doi.org/10.1016/j.foodchem.2007.05.077

[26]. Hollander, P. Drugs 1992, 44, 47-79.
https://doi.org/10.2165/00003495-199200443-00007

[27]. Toeller, M. Eur. J. Clin. Invest. 1994, 24, 31-35.
https://doi.org/10.1111/j.1365-2362.1994.tb02253.x

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