Evaluation of acetylcholinesterase and carbonic anhydrase inhibition profiles of 1,2,3,4,6-pentasubstituted-4-hydroxy-cyclohexanes
2017; Wiley; Volume: 31; Issue: 9 Linguagem: Inglês
10.1002/jbt.21938
ISSN1099-0461
AutoresÜmit M. Koçyiğit, Parham Taslımı, Hayreddin Gezegen, İlhami Gülçın, Mustafa Ceylan,
Tópico(s)Phenothiazines and Benzothiazines Synthesis and Activities
ResumoJournal of Biochemical and Molecular ToxicologyVolume 31, Issue 9 e21938 RESEARCH ARTICLE Evaluation of acetylcholinesterase and carbonic anhydrase inhibition profiles of 1,2,3,4,6-pentasubstituted-4-hydroxy-cyclohexanes Umit M. Kocyigit, Corresponding Author Umit M. Kocyigit ukocyigit@cumhuriyet.edu.tr orcid.org/0000-0001-8710-2912 Vocational School of Health Services, Cumhuriyet University, Sivas, Turkey Correspondence Umit M. Kocyigit, Vocational School of Health Services, Cumhuriyet University, 58140 Sivas, Turkey. E-mail: ukocyigit@cumhuriyet.edu.trSearch for more papers by this authorParham Taslimi, Parham Taslimi orcid.org/0000-0002-3171-0633 Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, TurkeySearch for more papers by this authorHayreddin Gezegen, Hayreddin Gezegen orcid.org/0000-0003-3602-7400 Department of Nutrition and Dietetics, Faculty of Health Sciences, Cumhuriyet University, Sivas, TurkeySearch for more papers by this authorİlhami Gulçin, İlhami Gulçin orcid.org/0000-0001-5993-1668 Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, TurkeySearch for more papers by this authorMustafa Ceylan, Mustafa Ceylan orcid.org/0000-0002-9184-4385 Department of Chemistry, Faculty of Arts and Sciences, Gaziosmanpasa University, Tokat, TurkeySearch for more papers by this author Umit M. Kocyigit, Corresponding Author Umit M. Kocyigit ukocyigit@cumhuriyet.edu.tr orcid.org/0000-0001-8710-2912 Vocational School of Health Services, Cumhuriyet University, Sivas, Turkey Correspondence Umit M. Kocyigit, Vocational School of Health Services, Cumhuriyet University, 58140 Sivas, Turkey. E-mail: ukocyigit@cumhuriyet.edu.trSearch for more papers by this authorParham Taslimi, Parham Taslimi orcid.org/0000-0002-3171-0633 Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, TurkeySearch for more papers by this authorHayreddin Gezegen, Hayreddin Gezegen orcid.org/0000-0003-3602-7400 Department of Nutrition and Dietetics, Faculty of Health Sciences, Cumhuriyet University, Sivas, TurkeySearch for more papers by this authorİlhami Gulçin, İlhami Gulçin orcid.org/0000-0001-5993-1668 Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, TurkeySearch for more papers by this authorMustafa Ceylan, Mustafa Ceylan orcid.org/0000-0002-9184-4385 Department of Chemistry, Faculty of Arts and Sciences, Gaziosmanpasa University, Tokat, TurkeySearch for more papers by this author First published: 14 June 2017 https://doi.org/10.1002/jbt.21938Citations: 40Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract Carbonic anhydrase (CA; EC 4.2.1.1) is used for remedial purposes for several years, as there is significant focus on expanding more new activators (CAAs) and high affinity inhibitors. Alzheimer′s disease and other similar ailments such as dementia and vascular dementia with Lewy bodies reduce cholinergic activity in the important areas involved in cognition and memory. Prevalent drugs for the symptomatic therapy of dementia are significant in increasing the associated cholinergic deficiency by inhibiting acetylcholinesterase (AChE). These six-membered carbocycles showed nice inhibitory action against AChE and human carbonic anhydrase (hCA) II and I isoforms. The hCA I, II, and AChE were efficiently inhibited by these molecules, with Ki values in the range of 6.70–35.85 nM for hCA I, 18.77–60.84 nM for hCA II, and 0.74–4.60 for AChE, respectively. Citing Literature Volume31, Issue9September 2017e21938 RelatedInformation
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