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dc.creatorBosak, Anita
dc.creatorOpsenica, Dejan
dc.creatorŠinko, Goran
dc.creatorZlatar, Matija
dc.creatorKovarik, Zrinka
dc.date.accessioned2019-05-30T01:17:48Z
dc.date.available2020-06-15
dc.date.issued2019
dc.identifier.issn0009-2797
dc.identifier.urihttps://cer.ihtm.bg.ac.rs/handle/123456789/2905
dc.description.abstractEight derivatives of 4-aminoquinolines differing in the substituents attached to the C(4)-amino group and C(7)were synthesised and tested as inhibitors of human acetylcholinesterase (AChE)and butyrylcholinesterase (BChE). Both enzymes were inhibited by all of the compounds with inhibition constants (K i )ranging from 0.50 to 50 μM exhibiting slight selectivity toward AChE over BChE. The most potent inhibitors of AChE were compounds with an n-octylamino chain or adamantyl group. The shortening of the chain length resulted in a decrease in AChE inhibition by 5–20 times. Docking studies revealed that the quinoline group within the AChE active site was positioned in the choline binding site, while the C(4)-amino group substituents, depending on their lipophilicity, could establish hydrogen bonds or π-interactions with residues of the peripheral anionic site. The most potent inhibitors of BChE were compounds with the most voluminous substituent on C(4)-amino group (adamantyl)or those with a stronger electron withdrawing substituent on C(7)(trifluormethyl group). Based on AChE inhibition, compounds with an n-octylamino chain or adamantyl substituent were shown to possess the capacity for further development as potential drugs for treatment of neurodegenerative diseases. © 2019 Elsevier B.V.en
dc.language.isoen
dc.publisherElsevier Ireland Ltd
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172035/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172008/RS//
dc.relationCroatian Science Foundation (IP-2018-01-7683)
dc.rightsembargoedAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceChemico-Biological Interactions
dc.subjectCholinesterase
dc.subjectAlzheimer's disease
dc.subjectpKa values
dc.subjectQuinoline-based compounds
dc.subjectselectivity
dc.subjectdocking
dc.subjectDFT
dc.titleStructural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesteraseen
dc.typearticleen
dc.rights.licenseBY-NC-ND
dcterms.abstractШинко, Горан; Опсеница, Дејан; Златар, Матија; Босак, Aнита; Коварик, Зринка;
dc.rights.holderElsevier
dc.citation.volume308
dc.citation.spage101
dc.citation.epage109
dc.citation.rankM21
dc.description.otherThis is peer-reviewed version of the article: [https://doi.org/10.1016/j.cbi.2019.05.024]
dc.description.other[http://cer.ihtm.bg.ac.rs/handle/123456789/2886]
dc.identifier.pmid31100281
dc.identifier.doi10.1016/j.cbi.2019.05.024
dc.identifier.fulltexthttps://cer.ihtm.bg.ac.rs/bitstream/id/7042/10.1016@j.cbi.2019.05.024.pdf
dc.identifier.scopus2-s2.0-85065775348
dc.identifier.wos000474214200010
dc.type.versionacceptedVersion


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