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Updated: Jul 16, 2026

Simultaneous Measurement of HDAC1 and HDAC6 Activity in HeLa Cells Using UHPLC-MS
Published on: August 10, 2017
Structural requirements of HDAC inhibitors: SAHA analogs functionalized adjacent to the hydroxamic acid
Anton V Bieliauskas1, Sujith V W Weerasinghe, Mary Kay H Pflum
1Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.
Abstract:
Inhibitors of histone deacetylase (HDAC) proteins such as suberoylanilide hydroxamic acid (SAHA) have emerged as effective therapeutic anti-cancer agents. To better understand the structural requirements of HDAC inhibitors, a small molecule library with a variety of substituents attached adjacent to the metal binding hydroxamic acid of SAHA was synthesized. The presence of a substituent adjacent to the hydroxamic acid led to an 800- to 5000-fold decrease in inhibition compared to SAHA. The observed results have implications for drug design, suggesting that HDAC inhibitors with substituents near the metal binding moiety will have inhibitory activities in the micromolar rather than nanomolar range.
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