|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Wagner, FF, Olson, DE, Gale, JP, Kaya, T, Weïwer, M, Aidoud, N, Thomas, M, Davoine, EL, Lemercier, BC, Zhang, Y-L, Holson, EB|
|Journal||J Med Chem|
|Date Published||2013 Feb 28|
|Keywords||HeLa Cells, Histone Deacetylase 6, Histone Deacetylase Inhibitors, Histone Deacetylases, Humans, Hydroxamic Acids, Isoenzymes, Molecular Mimicry, Protein Interaction Domains and Motifs, Structure-Activity Relationship|
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.
|Alternate Journal||J. Med. Chem.|