Yelekçi, KemalBora-Tatar, GamzeDayangac-Erden, DidemDemir, Ayhan S.Dalkara, SevimYelekçi, KemalErdem-Yurter, Hayat2019-06-272019-06-2720091450968-08961464-33910968-08961464-3391https://hdl.handle.net/20.500.12469/1096https://doi.org/10.1016/j.bmc.2009.05.042In the light of known HDAC inhibitors 33 carboxylic acid derivatives were tested to understand the structural requirements for HDAC inhibition activity. Several modifications were applied to develop the structure-activity relationships of carboxylic acid HDAC inhibitors. HDAC inhibition activities were investigated in vitro by using HeLa nuclear extract in a fluorimetric assay. Molecular docking was also carried out for the human HDAC8 enzyme in order to predict inhibition activity and the 3D poses of inhibitor-enzyme complexes. Of these compounds caffeic acid derivatives such as chlorogenic acid and curcumin were found to be highly potent compared to sodium butyrate which is a well-known HDAC inhibitor. (C) 2009 Elsevier Ltd. All rights reserved.eninfo:eu-repo/semantics/openAccessHDAC inhibitorsMolecular dockingCaffeic acid derivativesChlorogenic acidCurcuminCarboxylic acid derivativesMolecular modifications on carboxylic acid derivatives as potent histone deacetylase inhibitors: Activity and docking studiesArticle521952281417WOS:00026787300004410.1016/j.bmc.2009.05.0422-s2.0-67650078931Q2Q219520580