Peptidylarginine deiminases 4 as a promising target in drug discovery

  • Eur J Med Chem. 2021 Dec 15:226:113840. doi: 10.1016/j.ejmech.2021.113840.
Chao Yang  1 Zhen-Zhen Dong  2 Jing Zhang  1 Dehong Teng  1 Xinzhi Luo  1 Dan Li  3 Yingtang Zhou  4
Affiliations
  • 1. National Engineering Research Center for Marine Aquaculture, Institute of Innovation & Application, Zhejiang Ocean University, Zhoushan, Zhejiang Province, 316022, China.
  • 2. Department of Chemistry, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China.
  • 3. State Key Laboratory of Southwestern Chinese Medicine Resources, School of Pharmacy, Chengdu University of Traditional Chinese Medicine, Chengdu, China. Electronic address: [email protected].
  • 4. National Engineering Research Center for Marine Aquaculture, Institute of Innovation & Application, Zhejiang Ocean University, Zhoushan, Zhejiang Province, 316022, China. Electronic address: [email protected].
Abstract

Peptidylarginine deaminase 4 (PAD4) is a crucial post-translational modifying enzyme catalyzing the conversion of arginine into citrulline residues, and mediating the formation of neutrophil extracellular traps (NETs). PAD4 plays a vital role in the occurrence and development of cardiovascular diseases, autoimmune diseases, and various tumors. Therefore, PAD4 is considered as a promising drug target for disease diagnosis and treatment. More and more efforts are devoted to developing highly efficient and selective PAD4 inhibitors via high-throughput screening, structure-based drug design and structure-activity relationship study. This article outlined the physiological and pathological functions of PAD4, and corresponding representative small molecule inhibitors reported in recent years.

Keywords
Autoimmune disease; Citrullination; Histone; NETs; PAD4 inhibitor.