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Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin.
J Enzyme Inhib Med Chem. 2016; 31(3):441-7.JE

Abstract

Taxifolin, also known as dihydroquercetin, is a flavonoid commonly found in plants. Carbonic anhydrase (CA, EC 4.2.1.1) plays an important role in many critical physiological events including carbon dioxide (CO2)/bicarbonate (HCO3(-)) respiration and pH regulation. There are 16 known CA isoforms in humans, of which human hCA isoenzymes I and II (hCA I and II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of taxifolin against the slow cytosolic isoenzyme hCA I, and the ubiquitous and dominant rapid cytosolic isoenzyme hCA II were studied. Taxifolin, as a naturally bioactive flavonoid, has a K(i) of 29.2 nM against hCA I, and 24.2 nM against hCA II. For acetylcholinesterase enzyme (AChE) inhibition, K(i) parameter of taxifolin was determined to be 16.7 nM. These results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels.

Authors+Show Affiliations

a Central Researching Laboratory, Agri Ibrahim Cecen University , Agri , Turkey .b Department of Medical Services and Techniques, Vocational School of Health Services, Gumushane University , Gumushane , Turkey .b Department of Medical Services and Techniques, Vocational School of Health Services, Gumushane University , Gumushane , Turkey .c Department of Chemistry, Faculty of Sciences, Atatürk University , Erzurum , Turkey .c Department of Chemistry, Faculty of Sciences, Atatürk University , Erzurum , Turkey .c Department of Chemistry, Faculty of Sciences, Atatürk University , Erzurum , Turkey . d Zoology Department, College of Science, Fetal Programming of Diseases Research Chair, King Saud University , Riyadh , Saudi Arabia .d Zoology Department, College of Science, Fetal Programming of Diseases Research Chair, King Saud University , Riyadh , Saudi Arabia .e Dipartimento di Chimica Ugo Schiff, Universita degli Studi di Firenze , Sesto Fiorentino , Firenze , Italy , and. f Neurofarba Department, Section of Pharmaceutical and Nutriceutical Sciences, Universita degli Studi di Firenze , Sesto Fiorentino , Florence , Italy.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25893707

Citation

Gocer, Hulya, et al. "Acetylcholinesterase and Carbonic Anhydrase Isoenzymes I and II Inhibition Profiles of Taxifolin." Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 31, no. 3, 2016, pp. 441-7.
Gocer H, Topal F, Topal M, et al. Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin. J Enzyme Inhib Med Chem. 2016;31(3):441-7.
Gocer, H., Topal, F., Topal, M., Küçük, M., Teke, D., Gülçin, İ., Alwasel, S. H., & Supuran, C. T. (2016). Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(3), 441-7. https://doi.org/10.3109/14756366.2015.1036051
Gocer H, et al. Acetylcholinesterase and Carbonic Anhydrase Isoenzymes I and II Inhibition Profiles of Taxifolin. J Enzyme Inhib Med Chem. 2016;31(3):441-7. PubMed PMID: 25893707.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin. AU - Gocer,Hulya, AU - Topal,Fevzi, AU - Topal,Meryem, AU - Küçük,Murat, AU - Teke,Dilek, AU - Gülçin,İlhami, AU - Alwasel,Saleh H, AU - Supuran,Claudiu T, Y1 - 2015/04/20/ PY - 2015/4/21/entrez PY - 2015/4/22/pubmed PY - 2016/11/5/medline KW - Acetylcholinesterase KW - carbonic anhydrase KW - enzyme inhibition KW - enzyme purification KW - taxifolin SP - 441 EP - 7 JF - Journal of enzyme inhibition and medicinal chemistry JO - J Enzyme Inhib Med Chem VL - 31 IS - 3 N2 - Taxifolin, also known as dihydroquercetin, is a flavonoid commonly found in plants. Carbonic anhydrase (CA, EC 4.2.1.1) plays an important role in many critical physiological events including carbon dioxide (CO2)/bicarbonate (HCO3(-)) respiration and pH regulation. There are 16 known CA isoforms in humans, of which human hCA isoenzymes I and II (hCA I and II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of taxifolin against the slow cytosolic isoenzyme hCA I, and the ubiquitous and dominant rapid cytosolic isoenzyme hCA II were studied. Taxifolin, as a naturally bioactive flavonoid, has a K(i) of 29.2 nM against hCA I, and 24.2 nM against hCA II. For acetylcholinesterase enzyme (AChE) inhibition, K(i) parameter of taxifolin was determined to be 16.7 nM. These results clearly show that taxifolin inhibited both CA isoenzymes and AChE at the nM levels. SN - 1475-6374 UR - https://www.unboundmedicine.com/medline/citation/25893707/Acetylcholinesterase_and_carbonic_anhydrase_isoenzymes_I_and_II_inhibition_profiles_of_taxifolin_ L2 - http://www.tandfonline.com/doi/full/10.3109/14756366.2015.1036051 DB - PRIME DP - Unbound Medicine ER -