- Molecular modifications on carboxylic acid derivatives as potent histone deacetylase inhibitors: Activity and docking studies.
Molecular modifications on carboxylic acid derivatives as potent histone deacetylase inhibitors: Activity and docking studies.
Bioorganic & medicinal chemistry (2009-06-13)
Gamze Bora-Tatar, Didem Dayangaç-Erden, Ayhan S Demir, Sevim Dalkara, Kemal Yelekçi, Hayat Erdem-Yurter
PMID19520580
ABSTRACT
In 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.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
L-Valine, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, 98.5-101.0%
Sigma-Aldrich
Salicylic acid, meets analytical specification of Ph. Eur., BP, USP, 99.5-100.5% (calc. to the dried substance)
Sigma-Aldrich
8-Quinolinol, puriss. p.a., ACS reagent, reag. Ph. Eur., ≥99% (perchloric acid titration)
Supelco
L-Valine, certified reference material, TraceCERT®, Manufactured by: Sigma-Aldrich Production GmbH, Switzerland
Supelco
Salicylic acid, certified reference material, TraceCERT®, Manufactured by: Sigma-Aldrich Production GmbH, Switzerland
Chlorogenic acid, primary reference standard