Histone deacetylase (HDAC) is a type of metalloenzymes that removes acetyl groups from histone proteins found within DNA, therefore making DNA inaccessible for transcription. Research has shown that inhibition of HDAC triggers growth arrest, differentiation, and/or apoptosis in many types of tumor cells. HDAC (except class III) are known as Zn-dependent enzyme, therefore it is expected that inhibition of HDAC catalytic activity will be enhanced with the presence of a sulfur-containing group in an appropriate position. Herein we describe our recent findings in the identification and optimization of thioamide HDAC inhibitors. These compounds were synthesized through a three-step route, and computer modeling predicted stronger coordination between sulfur and zinc atom compared to their amide counterparts. These thioamides are undergoing biological assays to assess their effectiveness in cancer cells.

Histone deacetylase (HDAC) inhibitors containing thioamide: Synthesis and biological evaluation

249th National Meeting (2015)

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