Molecular docking and inhibition studies of vulpinic, carnosic and usnic acids on polyol pathway enzymes

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Aldose reductase (AR) and sorbitol dehydrogenase (SDH) are important enzymes of the polyol pathway. In the current study, inhibitory effects of vulpinic acid (VA) carnosic acid (CA) and usnic acid (UA) on purified AR and SDH enzymes were determined. These enzymes inhibition could be essential to prevent diabetic complications. AR and SDH enzymes were purified from sheep kidney. Then, VA, CA and UA were tested in various concentrations against these enzymes activity in vitro. K I values were found to be as 1.46 ± 0.04, 5.13 ± 0.25 and 11.71 ± 0.27 μΜ for VA, CA and UA, respectively, for AR. K I constants were found to be as 15.32 ± 0.34, 145.60 ± 2.17 and 213.40 ± 2.64 μΜ VA, CA and UA, respectively, for SDH. These findings indicate that VA, CA and UA could be useful in the treatment of diabetic complications. Communicated by Ramaswamy H. Sarma. © 2021 Informa UK Limited, trading as Taylor & Francis Group.

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AlanDeğerDil
dc.contributor.authorDemir, Yeliz
dc.contributor.authorCeylan, Hamid
dc.contributor.authorTürkeş, Cüneyt
dc.contributor.authorBeydemir, Şükrü
dc.date.accessioned2026-10-18T20:27:36.868418211Z
dc.date.available2026-10-18T20:27:36.868418211Z
dc.date.issued2022
dc.description.abstractAldose reductase (AR) and sorbitol dehydrogenase (SDH) are important enzymes of the polyol pathway. In the current study, inhibitory effects of vulpinic acid (VA) carnosic acid (CA) and usnic acid (UA) on purified AR and SDH enzymes were determined. These enzymes inhibition could be essential to prevent diabetic complications. AR and SDH enzymes were purified from sheep kidney. Then, VA, CA and UA were tested in various concentrations against these enzymes activity in vitro. K I values were found to be as 1.46 ± 0.04, 5.13 ± 0.25 and 11.71 ± 0.27 μΜ for VA, CA and UA, respectively, for AR. K I constants were found to be as 15.32 ± 0.34, 145.60 ± 2.17 and 213.40 ± 2.64 μΜ VA, CA and UA, respectively, for SDH. These findings indicate that VA, CA and UA could be useful in the treatment of diabetic complications. Communicated by Ramaswamy H. Sarma. © 2021 Informa UK Limited, trading as Taylor & Francis Group.
dc.description.sponsorshipThis work was supported by the Research Fund of Ardahan University [grant number 2019-008], the Research Fund of Erzincan Binali Yıldırım University [grant number FBA-2017-501] and the Research Fund of Anadolu University [grant number 2102S003].
dc.identifier.doi10.1080/07391102.2021.1967195
dc.identifier.eissn1538-0254
dc.identifier.endpage12021
dc.identifier.issn0739-1102
dc.identifier.issue22
dc.identifier.pmid34424822
dc.identifier.scopus2-s2.0-85113732400
dc.identifier.startpage12008
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/12749
dc.identifier.volume40
dc.identifier.wosWOS:000687604400001
dc.language.isoen
dc.publisherTaylor and Francis Ltd.
dc.relation.ispartofJournal of Biomolecular Structure and Dynamics
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAldose reductase
dc.subjectcarnosic acid
dc.subjectsorbitol dehydrogenase
dc.subjectusnic acid
dc.subjectvulpinic acid
dc.subjectAnimals
dc.subjectBenzofurans
dc.subjectL-Iditol 2-Dehydrogenase
dc.subjectMolecular Docking Simulation
dc.subjectPolymers
dc.subjectSheep
dc.subjectaldehyde reductase
dc.subjectammonium sulfate
dc.subjectiditol dehydrogenase
dc.subjectpolyol
dc.subjectbenzofuran derivative
dc.subjectpolymer
dc.subjectaffinity chromatography
dc.subjectanimal experiment
dc.subjectanion exchange chromatography
dc.subjectArticle
dc.subjectcomputer model
dc.subjectcontrolled study
dc.subjectdiabetic complication
dc.subjectdialysis
dc.subjectenzyme inhibition
dc.subjectgel filtration chromatography
dc.subjectmolecular docking
dc.subjectnonhuman
dc.subjectpolyacrylamide gel electrophoresis
dc.titleMolecular docking and inhibition studies of vulpinic, carnosic and usnic acids on polyol pathway enzymes
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus102
rdl.citation.wos101
rdl.departmentDepartment of Biochemistry, Faculty of Pharmacy, Erzincan Binali Yıldırım University, Erzincan, Turkey.
rdl.oa.statusgreen
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.source.indexPUBMED
rdl.wos.indexScience Citation Index Expanded (SCI-EXPANDED)