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Histone Deacetylases (HDAC) Targeted Library

9,500 Compounds

ChemDiv’s Histone Deacetylases (HDAC) Targeted Library contains 9,500 compounds.

Regulation of gene expression is mediated by several mechanisms such as DNA methylation, ATP-dependent chromatin remodeling, and post-translational modifications of histones. The latter mechanism includes dynamic acetylation and deacetylation of ε-amino groups of lysine residues present in the tail of the core histones. Histones are the predominant protein components of chromatin, which stabilize the nucleosome core. They are subjected to a variety of specific post-translational modifications. Reversible acetylation and deacetylation of nucleosomal histones are critical in the modulation of chromatin structure, chromatin function and in the regulation of gene expression. Enzymes responsible for the reversible acetylation/deacetylation processes are histone acetyltransferase (HATs) and histone deacetylases (HDACs), respectively.

Relatively modest progress in understanding pharmacology and clinical role of HDACs has been made since their discovery. Further optimization of these molecules into clinical candidates may yield drugs with enhanced efficacy against cancers, neurodegenerative and inflammatory diseases.

HDAC Targeted Library Selection_examples

Medicinal and Computational Chemistry Dept., ChemDiv, Inc.
12760 High Bluff Dr, San Diego, CA, 92130
Phone: + 1 916 234 0888
Fax: +1 858 794 4931
Email: ChemDiv@chemdiv.com

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