Aurones as histone deacetylase inhibitors: identification of key features

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dc.contributor.authorZwick, V.
dc.contributor.authorChatzivasileiou, A.-O.
dc.contributor.authorDeschamps, N.
dc.contributor.authorRoussaki, M.
dc.contributor.authorSimões-Pires, C.A.
dc.contributor.authorNurisso, A.
dc.contributor.authorDenis, I.
dc.contributor.authorBlanquart, C.
dc.contributor.authorMartinet, N.
dc.contributor.authorCarrupt, P.-A.
dc.contributor.authorDetsi, A.
dc.contributor.authorCuendet, M.
dc.date.issued2014
dc.description.abstractIn this study, a total of 22 flavonoids were tested for their HDAC inhibitory activity using fluorimetric and BRET-based assays. Four aurones were found to be active in both assays and showed IC50 values below 20 μM in the enzymatic assay. Molecular modelling revealed that the presence of hydroxyl groups was responsible for good compound orientation within the isoenzyme catalytic site and zinc chelation.
dc.description.statementofresponsibilityVincent Zwick, Alkiviadis-Orfefs Chatzivasileiou, Nathalie Deschamps, Marina Roussaki, Claudia A. Simões-Pires ... Iza Denis ... et al.
dc.identifier.citationBioorganic and Medicinal Chemistry Letters, 2014; 24(23):5497-5501
dc.identifier.doi10.1016/j.bmcl.2014.10.019
dc.identifier.issn0960-894X
dc.identifier.issn1464-3405
dc.identifier.orcidDenis, I. [0000-0002-2882-4306]
dc.identifier.urihttp://hdl.handle.net/2440/118656
dc.language.isoen
dc.publisherElsevier
dc.rights© 2014 Elsevier Ltd. All rights reserved.
dc.source.urihttps://doi.org/10.1016/j.bmcl.2014.10.019
dc.subjectHistone deacetylase; structure activity relationship; docking; aurone
dc.titleAurones as histone deacetylase inhibitors: identification of key features
dc.typeJournal article
pubs.publication-statusPublished

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