journal article

Journal Article

Text

Journal of Medicinal Chemistry. 2023, 66(17), p. 11672-11700

Evolution of Slow-Binding Inhibitors Targeting Histone Deacetylase Isoforms

American Chemical Society

English

Text

2023-09-14

https://doi.org/10.1021/acs.jmedchem.3c01160

Mukherjee A., Zamani F., Suzuki T.. Evolution of Slow-Binding Inhibitors Targeting Histone Deacetylase Isoforms. Journal of Medicinal Chemistry 66, 11672 (2023); https://doi.org/10.1021/acs.jmedchem.3c01160.

Because the overexpression of histone deacetylase enzymes (HDACs) has been linked to numerous diseases, including various cancers and neurodegenerative disorders, HDAC inhibitors have emerged as promising therapeutic agents. However, most HDAC inhibitors lack both subclass and isoform selectivity, which leads to potential toxicity. Unlike classical hydroxamate HDAC inhibitors, slow-binding HDAC inhibitors form tight and prolonged bonds with HDAC enzymes. This distinct mechanism of action improves both selectivity and toxicity profiles, which makes slow-binding HDAC inhibitors a promising class of therapeutic agents for various diseases. Therefore, the development of slow-binding HDAC inhibitors that can effectively target a wide range of HDAC isoforms is crucial. This Perspective provides valuable insights into the potential and progress of slow-binding HDAC inhibitors as promising drug candidates for the treatment of various diseases.

This document is the Accepted Manuscript version of a Published Work that appeared in final form inJournal of Medicinal Chemistry, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jmedchem.3c01160.

93985

Evolution of Slow-Binding Inhibitors Targeting Histone Deacetylase Isoforms

American Chemical Society

English

2023-09-14

Journal of Medicinal Chemistry

66

17

11672

11700

https://doi.org/10.1021/acs.jmedchem.3c01160

https://hdl.handle.net/11094/93985