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Potent and selective inhibition of histone deacetylase 6 (HDAC6) does not require a surface-binding motif.
Wagner, Florence F; Olson, David E; Gale, Jennifer P; Kaya, Taner; Weïwer, Michel; Aidoud, Nadia; Thomas, Méryl; Davoine, Emeline L; Lemercier, Bérénice C; Zhang, Yan-Ling; Holson, Edward B.
Affiliation
  • Wagner FF; Stanley Center for Psychiatric Research, Broad Institute of MIT and Harvard, Cambridge, Massachusetts 02142, United States.
J Med Chem ; 56(4): 1772-6, 2013 Feb 28.
Article in En | MEDLINE | ID: mdl-23368884
Hydroxamic acids were designed, synthesized, and evaluated for their ability to selectively inhibit human histone deacetylase 6 (HDAC6). Several inhibitors, including compound 14 (BRD9757), exhibited excellent potency and selectivity despite the absence of a surface-binding motif. The binding of these highly efficient ligands for HDAC6 is rationalized via structure-activity relationships. These results demonstrate that high selectivity and potent inhibition of HDAC6 can be achieved through careful choice of linker element only.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Histone Deacetylase Inhibitors / Histone Deacetylases / Hydroxamic Acids Limits: Humans Language: En Journal: J Med Chem Journal subject: QUIMICA Year: 2013 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Histone Deacetylase Inhibitors / Histone Deacetylases / Hydroxamic Acids Limits: Humans Language: En Journal: J Med Chem Journal subject: QUIMICA Year: 2013 Document type: Article Affiliation country: Country of publication: