Design, synthesis and biological evaluation of quinoline-2-carbonitrile-based hydroxamic acids as dual tubulin polymerization and histone deacetylases inhibitors

Eur J Med Chem. 2022 Oct 5:240:114573. doi: 10.1016/j.ejmech.2022.114573. Epub 2022 Jul 1.

Abstract

A series of quinoline and quinazoline analogs were designed and synthesized as new tubulin polymerization (TP) and histone deacetylases (HDAC) inhibitors. Compounds 12a and 12d showed the best cytotoxicity activities against a panel of human cancer cell lines with an averaged IC50 value of 0.6 and 0.7 nM, respectively. Furthermore, these lead compounds showed good activities against CA-4-resistant colon-carcinoma and multidrug-resistant leukemia cells. In addition, compounds 12a and 12d induced HT29 cell cycle arrest in the G2/M phase and produced caspase-induced apoptosis of HT29 cells through mitochondrial dysfunction. Also, 12a and 12d inhibited HDAC8, 6, and 11 activities. Furthermore, lead compound 12a exhibited higher metabolic stability than isoCA-4 and was highly potent in suppressing tumor growth in the fibrosarcoma MCA205 tumor model. Collectively, these studies suggest that 12a represents a new dual inhibitor of TP and HDAC activities, which makes it a suitable candidate for further investigations in clinical development.

Keywords: Cancer; Cytotoxicity; HDACi; Multitargeted compounds; Tubulin.

MeSH terms

  • Antineoplastic Agents*
  • Cell Line, Tumor
  • Cell Proliferation
  • Drug Design
  • Drug Screening Assays, Antitumor
  • Histone Deacetylase Inhibitors / pharmacology
  • Histone Deacetylases / metabolism
  • Humans
  • Hydroxamic Acids / pharmacology
  • Polymerization
  • Quinolines* / pharmacology
  • Repressor Proteins
  • Tubulin / metabolism

Substances

  • Antineoplastic Agents
  • Histone Deacetylase Inhibitors
  • Hydroxamic Acids
  • Quinolines
  • Repressor Proteins
  • Tubulin
  • HDAC8 protein, human
  • Histone Deacetylases