Your browser doesn't support javascript.
loading
Mercaptoacetamide: A promising zinc-binding group for the discovery of selective histone deacetylase 6 inhibitors.
Tavares, Maurício T; Kozikowski, Alan P; Shen, Sida.
Afiliación
  • Tavares MT; Department of Molecular Medicine, Scripps Research, Jupiter, FL, 33458, United States.
  • Kozikowski AP; Bright Minds Biosciences, Toronto, ON, M5H 3V9, Canada.
  • Shen S; Departments of Chemistry, Chemistry of Life Processes Institute, Center for Molecular Innovation and Drug Discovery, And Center for Developmental Therapeutics, Northwestern University, Evanston, IL 60208, United States. Electronic address: sida.shen@northwestern.edu.
Eur J Med Chem ; 209: 112887, 2021 Jan 01.
Article en En | MEDLINE | ID: mdl-33035922
Histone deacetylase 6 (HDAC6) is a zinc-dependent HDAC that mainly modulates the acetylation status of non-histone substrates, such as α-tubulin and heat shock protein 90 (HSP90). The activity of HDAC6 plays a critical role in cell proliferation, protein trafficking and degradation, cell shape, migration, as well as regulation of immunomodulatory factors. For this reason, HDAC6 influences the progress of cancers, neurodegenerative disorders, and autoimmune responses. In the last few years, the discovery of selective HDAC6 inhibitors (HDAC6is) has become an attractive research area as five HDAC6is are being investigated in phase I/II clinical trials. However, the hydroxamic acid functional group still represents the predominant zinc-binding group (ZBG), that often suffers from poor pharmacokinetics and mutagenic potential, thus impairing the application of hydroxamate-based HDAC6is for long-term therapies. On the other hand, mercaptoacetamide (MCA)-based HDAC6is comprise a class of compounds that, in some cases, display nanomolar HDAC6 potency and a thousand-fold selectivity over class I HDAC isozymes. Moreover, MCA-based HDAC6is lack the mutagenicity associated with the hydroxamate function and display pharmacological effects, demonstrating the potential of this particular ZBG to improve upon the drug-like properties of HDAC6is. Herein, we summarize for the first time the structure-activity relationships (SARs) of MCA-based HDAC6is, discuss their HDAC6 selectivity at the molecular level using inhibitor-HDAC co-crystal structures, and further provide our perspective regarding their drug metabolism, pharmacokinetics, and pharmacological properties.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Compuestos de Sulfhidrilo / Inhibidores de Histona Desacetilasas / Histona Desacetilasa 6 Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Eur J Med Chem Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Francia

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Compuestos de Sulfhidrilo / Inhibidores de Histona Desacetilasas / Histona Desacetilasa 6 Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Eur J Med Chem Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Francia