Identification of new NIK inhibitors by discriminatory analysis-based molecular docking and biological evaluation

Arch Pharm (Weinheim). 2019 Jul;352(7):e1800374. doi: 10.1002/ardp.201800374. Epub 2019 May 22.

Abstract

NF-κB inducing kinase (NIK) is a key regulator in the noncanonical nuclear factor κB cells (NF-κB) signaling pathway. Dysregulation of NIK is often related with autoimmune disorders and malignancies. However, the number of reported NIK inhibitors is scarce. Discriminatory analysis-based molecular docking was used to examine the accuracy of the binding conformation and to estimate the binding affinity, leading to the identification of several new NIK inhibitors with moderate IC50 (ranging from 48.9 to 103.4 μM). Among them, compound 5, the most potent one (IC50 48.9 ± 6.9 μM), also showed moderate antiproliferation activity against cancer SW1990 cells, with an IC50 value of 20.1 ± 6.0 μM. Further dynamic simulations were performed to provide more in-depth details on the binding conformation of compound 5 and the NIK protein, providing some structural clues for further optimization of compound 5 as a novel NIK inhibitor.

Keywords: NF-κB inducing kinase; antiproliferation activity; inhibitors; virtual screen.

MeSH terms

  • Dose-Response Relationship, Drug
  • Humans
  • Molecular Docking Simulation*
  • Molecular Structure
  • NF-kappaB-Inducing Kinase
  • Protein Kinase Inhibitors / chemical synthesis
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / pharmacology*
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / metabolism
  • Structure-Activity Relationship

Substances

  • Protein Kinase Inhibitors
  • Protein Serine-Threonine Kinases