A Review of Progress in Histone Deacetylase 6 Inhibitors Research: Structural Specificity and Functional Diversity

Histone deacetylases (HDACs) are essential for maintaining homeostasis by catalyzing histone deacetylation. Aberrant expression of HDACs is associated with various human diseases. Although HDAC inhibitors are used as effective chemotherapeutic agents in clinical practice, their applications remain l...

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Published inJournal of medicinal chemistry Vol. 64; no. 3; pp. 1362 - 1391
Main Authors Zhang, Xin-Hui, Qin-Ma, Wu, Hui-Pan, Khamis, Mussa Yussuf, Li, Yi-Han, Ma, Li-Ying, Liu, Hong-Min
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 11.02.2021
Subjects
Animals
Histone Deacetylase 6 - antagonists & inhibitors
Histone Deacetylase Inhibitors - chemistry
Histone Deacetylase Inhibitors - pharmacology
Histone Deacetylase Inhibitors - therapeutic use
Histone Deacetylases - chemistry
Humans
Models, Molecular
Structure-Activity Relationship
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Abstract Histone deacetylases (HDACs) are essential for maintaining homeostasis by catalyzing histone deacetylation. Aberrant expression of HDACs is associated with various human diseases. Although HDAC inhibitors are used as effective chemotherapeutic agents in clinical practice, their applications remain limited due to associated side effects induced by weak isoform selectivity. HDAC6 displays unique structure and cellular localization as well as diverse substrates and exhibits a wider range of biological functions than other isoforms. HDAC6 inhibitors have been effectively used to treat cancers, neurodegenerative diseases, and autoimmune disorders without exerting significant toxic effects. Progress has been made in defining the crystal structures of HDAC6 catalytic domains which has influenced the structure-based drug design of HDAC6 inhibitors. This review summarizes recent literature on HDAC6 inhibitors with particular reference to structural specificity and functional diversity. It may provide up-to-date guidance for the development of HDAC6 inhibitors and perspectives for optimization of therapeutic applications.
AbstractList Histone deacetylases (HDACs) are essential for maintaining homeostasis by catalyzing histone deacetylation. Aberrant expression of HDACs is associated with various human diseases. Although HDAC inhibitors are used as effective chemotherapeutic agents in clinical practice, their applications remain limited due to associated side effects induced by weak isoform selectivity. HDAC6 displays unique structure and cellular localization as well as diverse substrates and exhibits a wider range of biological functions than other isoforms. HDAC6 inhibitors have been effectively used to treat cancers, neurodegenerative diseases, and autoimmune disorders without exerting significant toxic effects. Progress has been made in defining the crystal structures of HDAC6 catalytic domains which has influenced the structure-based drug design of HDAC6 inhibitors. This review summarizes recent literature on HDAC6 inhibitors with particular reference to structural specificity and functional diversity. It may provide up-to-date guidance for the development of HDAC6 inhibitors and perspectives for optimization of therapeutic applications.Histone deacetylases (HDACs) are essential for maintaining homeostasis by catalyzing histone deacetylation. Aberrant expression of HDACs is associated with various human diseases. Although HDAC inhibitors are used as effective chemotherapeutic agents in clinical practice, their applications remain limited due to associated side effects induced by weak isoform selectivity. HDAC6 displays unique structure and cellular localization as well as diverse substrates and exhibits a wider range of biological functions than other isoforms. HDAC6 inhibitors have been effectively used to treat cancers, neurodegenerative diseases, and autoimmune disorders without exerting significant toxic effects. Progress has been made in defining the crystal structures of HDAC6 catalytic domains which has influenced the structure-based drug design of HDAC6 inhibitors. This review summarizes recent literature on HDAC6 inhibitors with particular reference to structural specificity and functional diversity. It may provide up-to-date guidance for the development of HDAC6 inhibitors and perspectives for optimization of therapeutic applications.
Histone deacetylases (HDACs) are essential for maintaining homeostasis by catalyzing histone deacetylation. Aberrant expression of HDACs is associated with various human diseases. Although HDAC inhibitors are used as effective chemotherapeutic agents in clinical practice, their applications remain limited due to associated side effects induced by weak isoform selectivity. HDAC6 displays unique structure and cellular localization as well as diverse substrates and exhibits a wider range of biological functions than other isoforms. HDAC6 inhibitors have been effectively used to treat cancers, neurodegenerative diseases, and autoimmune disorders without exerting significant toxic effects. Progress has been made in defining the crystal structures of HDAC6 catalytic domains which has influenced the structure-based drug design of HDAC6 inhibitors. This review summarizes recent literature on HDAC6 inhibitors with particular reference to structural specificity and functional diversity. It may provide up-to-date guidance for the development of HDAC6 inhibitors and perspectives for optimization of therapeutic applications.
Author Ma, Li-Ying
Khamis, Mussa Yussuf
Liu, Hong-Min
Qin-Ma
Wu, Hui-Pan
Zhang, Xin-Hui
Li, Yi-Han
AuthorAffiliation China Meheco Topfond Pharmaceutical Co., Ltd
Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
AuthorAffiliation_xml – name: Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
– name: China Meheco Topfond Pharmaceutical Co., Ltd
Author_xml – sequence: 1
  givenname: Xin-Hui
  surname: Zhang
  fullname: Zhang, Xin-Hui
  organization: Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
– sequence: 2
  surname: Qin-Ma
  fullname: Qin-Ma
  organization: Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
– sequence: 3
  givenname: Hui-Pan
  surname: Wu
  fullname: Wu, Hui-Pan
  organization: Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
– sequence: 4
  givenname: Mussa Yussuf
  surname: Khamis
  fullname: Khamis, Mussa Yussuf
  organization: Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
– sequence: 5
  givenname: Yi-Han
  surname: Li
  fullname: Li, Yi-Han
  organization: Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
– sequence: 6
  givenname: Li-Ying
  orcidid: 0000-0002-7186-8259
  surname: Ma
  fullname: Ma, Li-Ying
  email: maliying@zzu.edu.cn
  organization: China Meheco Topfond Pharmaceutical Co., Ltd
– sequence: 7
  givenname: Hong-Min
  orcidid: 0000-0001-6771-9421
  surname: Liu
  fullname: Liu, Hong-Min
  email: liuhm@zzu.edu.cn
  organization: Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, Key Laboratory of Technology Drug Preparation (Zhengzhou University), Ministry of Education of China, Key Laboratory of Henan Province for Drug Quality and Evaluation; School of Pharmaceutical Sciences
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SecondaryResourceType review_article
Snippet Histone deacetylases (HDACs) are essential for maintaining homeostasis by catalyzing histone deacetylation. Aberrant expression of HDACs is associated with...
SourceID proquest
pubmed
crossref
acs
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 1362
SubjectTerms Animals
Histone Deacetylase 6 - antagonists & inhibitors
Histone Deacetylase Inhibitors - chemistry
Histone Deacetylase Inhibitors - pharmacology
Histone Deacetylase Inhibitors - therapeutic use
Histone Deacetylases - chemistry
Humans
Models, Molecular
Structure-Activity Relationship
Title A Review of Progress in Histone Deacetylase 6 Inhibitors Research: Structural Specificity and Functional Diversity
URI http://dx.doi.org/10.1021/acs.jmedchem.0c01782
https://www.ncbi.nlm.nih.gov/pubmed/33523672
https://www.proquest.com/docview/2485513189
Volume 64
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