An azumamide C analogue without the zinc-binding functionality?
MedChemComm Pub Date: 2014-08-12 DOI: 10.1039/C4MD00252K
Abstract
Histone deacetylase (HDAC) inhibitors have attracted considerable attention due to their promise as therapeutic agents. Most HDAC inhibitors adhere to a general “cap-linker-Zn2+-binding group” architecture but recent studies have indicated that potent inhibition may be achieved without a Zn2+-coordinating moiety. Herein, we describe the synthesis of an azumamide analogue lacking its native Zn2+-binding group and evaluation of its inhibitory activity against recombinant human HDAC1–11. Furthermore, kinetic investigation of the inhibitory mechanism of both parent natural product and synthetic analogue against HDAC3-NCoR2 is reported as well as their activity against Burkitt's lymphoma cell proliferation.
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Journal Name:MedChemComm
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CAS no.: 89640-58-4