In vitro antioxidant activity and carbonic anhydrase inhibitory features of Ferula communis extracts
Year 2021,
Volume: 5 Issue: 4, 592 - 598, 15.12.2021
Fatma Aydın
,
Zeynep Aleyna Kahraman
,
Emir Alper Türkoğlu
,
Müslüm Kuzu
,
Zeki Severoğlu
Abstract
Carbonic anhydrases (CAs; EC 4.2.1.1) are essential family of metalloenzymes which catalyze the interconversion between carbon dioxide (CO2) and bicarbonate (HCO3-) in all organisms of three-domains of life. Huge amounts of attempts related to catalytic activity of CAs have been widely expanded to treat many clinical diseases. This study aimed to determine in-vitro antioxidant activities and human CA I (hCA I) and II (hCA II) inhibitory properties of Ferula communis extracts. Among all extracts of F. communis, the hexane extract has showed the best inhibitory profile on hCA I and II with IC50 values 8.68 µg/mL and 28 µg/mL and Ki values 2.026 µg/mL and 11.6 µg/mL, respectively. All extracts showed mild to moderate antioxidant activity. According to the results of DPPH assay, ethanol-water extract showed the highest activity with IC50: 0.1128±0.0066 value. Chloroform extract showed the highest activity on CUPRAC assay with the value of 1.305±0.037 mM Trolox equivalent/mg extract. However, further analytical, in-vivo and clinical studies are needed to confirm the activities of F. communis.
Supporting Institution
TÜBİTAK and Scientific Research Project Fund of the University of Health Sciences Turkey
Project Number
TUBITAK 2209-A University Students Research Projects Support Program for Zeynep Aleyna KAHRAMAN and Scientific Research Project Fund of the University of Health Sciences Turkey under project number 2018/011.
Thanks
We also would like to thank our collaborator, Assoc. Prof. Dr. Turgut TAŞKIN, for his excellent recommendations.
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Year 2021,
Volume: 5 Issue: 4, 592 - 598, 15.12.2021
Fatma Aydın
,
Zeynep Aleyna Kahraman
,
Emir Alper Türkoğlu
,
Müslüm Kuzu
,
Zeki Severoğlu
Project Number
TUBITAK 2209-A University Students Research Projects Support Program for Zeynep Aleyna KAHRAMAN and Scientific Research Project Fund of the University of Health Sciences Turkey under project number 2018/011.
References
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- Aggarwal, M., Boone, C. D., Kondeti, B., McKenna, R. (2013). Structural annotation of human carbonic anhydrases. Journal of Enzyme Inhibition and Medicinal Chemistry, 28(2), 267-277. Doi: https://doi.org/10.3109/14756366.2012.737323
- Ağgül, A., Kuzu, M., Kandemir, F., Küçükler, S., Çağlayan, C. (2020). Alterations in enzyme activity of carbonic anhydrase, 6-phosphogluconate dehydrogenase and thioredoxin reductase in rats exposed to doxorubicin and morin. Clinical and Experimental Health Sciences, 10(3), 228-234. Retrieved from https://dergipark.org.tr/en/pub/clinexphealthsci/issue/56955/632320
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- Arnoldi, L., Ballero, M., Fuzzati, N., Maxia, A., Mercalli, E., Pagni, L. (2004). HPLC-DAD-MS identification of bioactive secondary metabolites from Ferula communis roots. Fitoterapia, 75(3-4), 342-354. Doi: https://doi.org/10.1016/j.fitote.2004.03.001
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- Balaydin, H. T., Durdaği, S., Ekinci, D., Şentürk, M., Göksu, S., Menzek, A. (2012). Inhibition of human carbonic anhydrase isozymes I, II and VI with a series of bisphenol, methoxy and bromophenol compounds. Journal of Enzyme Inhibition and Medicinal Chemistry, 27(4), 467-475. Doi: https://doi.org/10.3109/14756366.2011.596836
- Carta, F., Ferraroni, M., Scozzafava, A., Supuran, C. T. (2016). Fluorescent sulfonamide carbonic anhydrase inhibitors incorporating 1,2,3-triazole moieties: Kinetic and X-ray crystallographic studies. Bioorganic & Medicinal Chemistry, 24(2), 104-112. Doi: https://doi.org/10.1016/j.bmc.2015.11.031
- Ceruso, M., Antel, S., Vullo, D., Scozzafava, A., Supuran, C. T. (2014). Inhibition studies of new ureido-substituted sulfonamides incorporating a GABA moiety against human carbonic anhydrase isoforms I-XIV. Bioorganic & Medicinal Chemistry, 22(24), 6768-6775. Doi: https://doi.org/10.1016/j.bmc.2014.10.041
- Ceylan, S., Cetin, S., Camadan, Y., Saral, O., Ozsen, O., Tutus, A. (2019). Antibacterial and antioxidant activities of traditional medicinal plants from the Erzurum region of Turkey. Irish Journal of Medical Science, 188(4), 1303-1309. Doi: https://doi.org/10.1007/s11845-019-01993-x
- Çetinkaya, Y., Göçer, H., Gülçin, İ., Menzek, A. (2014). Synthesis and carbonic anhydrase isoenzymes ınhibitory effects of brominated diphenylmethanone and ıts derivatives. Archiv Der Pharmazie, 347(5), 354-359. Doi: https://doi.org/10.1002/ardp.201300349
- De Simone, G., Supuran, C. T. (2012). (In)organic anions as carbonic anhydrase inhibitors. Journal of Inorganic Biochemistry, 111, 117-129. Doi: https://doi.org/10.1016/j.jinorgbio.2011.11.017
- Ekinci, D., Çavdar, H., Talaz, O., Şentürk, M., Supuran, C. T. (2010). NO-releasing esters show carbonic anhydrase inhibitory action against human isoforms I and II. Bioorganic & Medicinal Chemistry, 18(10), 3559-3563. Doi: https://doi.org/10.1016/j.bmc.2010.03.082
- Fu, W., Chen, J., Cai, Y., Lei, Y., Chen, L., Pei, L., Zhou, D., Liang, X., Ruan, J. (2010). Antioxidant, free radical scavenging, anti-inflammatory and hepatoprotective potential of the extract from Parathelypteris nipponica (Franch. et Sav.) Ching. Journal of Ethnopharmacology, 130(3), 521–528. Doi: https://doi.org/10.1016/j.jep.2010.05.039
- Gençer, N., Bilen, Ç., Demir, D., Atahan, A., Ceylan, M., Küçükislamoğlu, M. (2013). In vitro inhibition effect of some chalcones on erythrocyte carbonic anhydrase I and II. Artificial Cells, Nanomedicine, and Biotechnology, 41(6), 384-388. Doi: https://doi.org/10.3109/21691401.2012.761226
Güney, M., Çavdar, H., Şentürk, M., Ekinci, D. (2015). Synthesis and carbonic anhydrase inhibitory properties of novel uracil derivatives. Bioorganic & Medicinal Chemistry Letters, 25(16), 3261-3263. Doi: https://doi.org/10.1016/j.bmcl.2015.05.073
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