Martin Luther University Halle-Wittenberg

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Fereshteh Mahmoudi

M.Sc. Fereshteh Mahmoudi

Tel. ++49 345 55 25188
email: fereshteh.mahmoudi85(at)

Development and biological characterization of novel HDAC11 inhibitors

Histone deacetylase 11 (HDAC11) preferentially removes fatty acid residues from lysine side chains in a peptideor protein environment. In the current project we aim to develop novel chemical probes for studying HDAC11. For this prupose combination of structure-based design, synthesis and the usage of a continuous fluorescence-based activity assay will be applied. By modifying TNFa peptides we recently identified a substrate [1] that enables fluorescence-based direct and continuous readout of HDAC11-mediated amide bond cleavage fully compatible with high-throughput screening formats.  In the absence of NAD+, this substrate is specific for HDAC11. Reevaluation of inhibitory data using our novel assay revealed limited potency and selectivity of known HDAC inhibitors. As best hit Elevenostat, a putative HDAC11-specific inhibitor, was identified.

1. Kutil Z, Mikešová J, Zessin M, Meleshin M, Nováková Z, Alquicer G, Kozikowski A, Sippl W, Bařinka C, Schutkowski M. Continuous Activity Assay for HDAC11 Enabling Reevaluation of HDAC Inhibitors. ACS Omega. 2019 Nov 15;4(22):19895-19904. doi: 10.1021/acsomega.9b02808.