Activation and inhibition effects of some natural products on human cytosolic CAI and CAII

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dc.authoridAdem, Sevki/0000-0003-2146-5870
dc.authoridaksit, Huseyin/0000-0002-1509-851X
dc.contributor.authorAdem, Sevki
dc.contributor.authorAkkemik, Ebru
dc.contributor.authorAksit, Huseyin
dc.contributor.authorGuller, Pinar
dc.contributor.authorTufekci, Ali Riza
dc.contributor.authorDemirtas, Ibrahim
dc.contributor.authorCiftci, Mehmet
dc.date.accessioned2024-12-24T19:24:23Z
dc.date.available2024-12-24T19:24:23Z
dc.date.issued2019
dc.departmentSiirt Üniversitesi
dc.description.abstractCarbonic anhydrases (CAs) play a significant function in diverse pathological and physiological processes. Their inhibitors and activators are suitable molecules to use as a drug in the treatment of different disease. In the present study, seven natural compounds, namely didymin, retusin isoquercitrin, silymarin, verbascoside, teucroside, and 3'-O-methylhypolaetin 7-O-[6'-O-acetyl-beta-D-allopyranosyl-(1 -> 2)]-6 ''-O-acetyl-beta-D-glucopyranoside were isolated from Mentha spicata, Sideritis libanotica linearis, Platanus orientalis, Teucrium chamaedrys subsp. chamaedrys, and Silybum marianum. The influences of compounds on the carbonic anhydrase I(hCAI) and II(hCAII) purified from human erythrocytes were tested. Five phenolic compounds acted as an inhibitor on the activity of hCAI, and IC50 values were computed between 18.16 and 172.5 mu M. Isozyme hCAII is only inhibited by silymarin with an IC50 value of 43.12 mu M. This isoenzyme was effectively activated by five natural compounds with AC(50) values in the range of 2.98-18.53 mu M. To understand the binding patterns of molecules that show activation effect against hCAII, molecular docking was done using Leadit 2.3.2 software, and calculated between -19.05 and -14.42 (kJ/mol) binding energies. Both in vitro and in silico results demonstrated that the best activators against hCAII were teucroside and isoquercitrin, with AC(50) values of 2.98 and 3.17 mu M, and binding energies -19.05 and -18.01 (kJ/mol), respectively. According to the ADME results, retusin demonstrated physicochemical and pharmacokinetic properties specific to the drug candidates.
dc.identifier.doi10.1007/s00044-019-02329-1
dc.identifier.endpage722
dc.identifier.issn1054-2523
dc.identifier.issn1554-8120
dc.identifier.issue5
dc.identifier.scopus2-s2.0-85064092041
dc.identifier.scopusqualityQ1
dc.identifier.startpage711
dc.identifier.urihttps://doi.org/10.1007/s00044-019-02329-1
dc.identifier.urihttps://hdl.handle.net/20.500.12604/5966
dc.identifier.volume28
dc.identifier.wosWOS:000464742900008
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherSpringer Birkhauser
dc.relation.ispartofMedicinal Chemistry Research
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_20241222
dc.subjectCarbonic anhydrase
dc.subjectNatural product
dc.subjectInhibition
dc.subjectActivation
dc.subjectDocking
dc.titleActivation and inhibition effects of some natural products on human cytosolic CAI and CAII
dc.typeArticle

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