Rapid identification of cholinesterase inhibitors from the seedcases of mangosteen using an enzyme affinity assay

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dc.contributor.authorHyung Won Ryu-
dc.contributor.authorSei-Ryang Oh-
dc.contributor.authorM J Curtis-Long-
dc.contributor.authorJ H Lee-
dc.contributor.authorHyuk Hwan Song-
dc.contributor.authorK H Park-
dc.date.accessioned2017-04-19T09:51:14Z-
dc.date.available2017-04-19T09:51:14Z-
dc.date.issued2014-
dc.identifier.issn00218561-
dc.identifier.uri10.1021/jf405072eko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11855-
dc.description.abstractEnzyme binding affinity has been recently introduced as a selective screening method to identify bioactive substances within complex mixtures. We used an assay which identified small molecule binders of acetylcholinesterase (AChE) using the following series of steps: incubation of enzyme with extract; centrifugation and filtration; identification of small molecule content in the flow through. The crude extract contained 10 peaks in the UPLC chromatogram. However, after incubation the enzyme, six peaks were reduced, indicating these compounds bound AChE. All these isolated compounds (2, 3, and 5-8) significantly inhibited human AChE with IC50s = 5.4-15.0 μM and butyrylcholinsterase (IC50s = 0.7-11.0 μM). All compounds exhibited reversible mixed kinetics. Consistent with the binding screen and fluorescence quenching, γ-mangostin 6 had a much higher affinity for AChE than 9-hydroxycalabaxanthone 9. This validates this screening protocol as a rapid method to identify inhibitors of AChE.-
dc.publisherAmer Chem Soc-
dc.titleRapid identification of cholinesterase inhibitors from the seedcases of mangosteen using an enzyme affinity assay-
dc.title.alternativeRapid identification of cholinesterase inhibitors from the seedcases of mangosteen using an enzyme affinity assay-
dc.typeArticle-
dc.citation.titleJournal of Agricultural and Food Chemistry-
dc.citation.number6-
dc.citation.endPage1343-
dc.citation.startPage1338-
dc.citation.volume62-
dc.contributor.affiliatedAuthorHyung Won Ryu-
dc.contributor.affiliatedAuthorSei-Ryang Oh-
dc.contributor.alternativeName류형원-
dc.contributor.alternativeName오세량-
dc.contributor.alternativeNameCurtis-Long-
dc.contributor.alternativeName이지혜-
dc.contributor.alternativeName송혁환-
dc.contributor.alternativeName박기훈-
dc.identifier.bibliographicCitationJournal of Agricultural and Food Chemistry, vol. 62, no. 6, pp. 1338-1343-
dc.identifier.doi10.1021/jf405072e-
dc.subject.keywordcholinesterase-
dc.subject.keywordenzyme binding affinity-
dc.subject.keywordfluorescence quenching-
dc.subject.keywordGarcinia mangostana-
dc.subject.keywordUPLC-PDA-QTOF-MS-
dc.subject.localcholinesterase-
dc.subject.localCholinesterase-
dc.subject.localenzyme binding affinity-
dc.subject.localfluorescence quenching-
dc.subject.localFluorescence quenching-
dc.subject.localGarcinia mangostana-
dc.subject.localUPLC-PDA-QTOF-MS-
dc.description.journalClassY-
Appears in Collections:
Ochang Branch Institute > Natural Medicine Research Center > 1. Journal Articles
Ochang Branch Institute > 1. Journal Articles
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