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Design and synthesis of novel histone deacetylase inhibitor derived from nuclear localization signal peptide.


ABSTRACT: We describe herein the synthesis and characterization of a new class of histone deacetylase (HDAC) inhibitors derived from conjugation of a suberoylanilide hydroxamic acid-like aliphatic-hydroxamate pharmacophore to a nuclear localization signal peptide. We found that these conjugates inhibited the histone deacetylase activities of HDACs 1, 2, 6, and 8 in a manner similar to suberoylanilide hydroxamic acid (SAHA). Notably, compound 7b showed a threefold improvement in HDAC 1/2 inhibition, a threefold increase in HDAC 6 selectivity and a twofold increase in HDAC 8 selectivity when compared to SAHA.

SUBMITTER: Canzoneri JC 

PROVIDER: S-EPMC2783919 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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Design and synthesis of novel histone deacetylase inhibitor derived from nuclear localization signal peptide.

Canzoneri Joshua C JC   Chen Po C PC   Oyelere Adegboyega K AK  

Bioorganic & medicinal chemistry letters 20091013 23


We describe herein the synthesis and characterization of a new class of histone deacetylase (HDAC) inhibitors derived from conjugation of a suberoylanilide hydroxamic acid-like aliphatic-hydroxamate pharmacophore to a nuclear localization signal peptide. We found that these conjugates inhibited the histone deacetylase activities of HDACs 1, 2, 6, and 8 in a manner similar to suberoylanilide hydroxamic acid (SAHA). Notably, compound 7b showed a threefold improvement in HDAC 1/2 inhibition, a thre  ...[more]

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