Vialinin A and thelephantin G, potent inhibitors of tumor necrosis factor-α production, inhibit sentrin/SUMO-specific protease 1 enzymatic activity

Bioorg Med Chem Lett. 2016 Sep 1;26(17):4237-40. doi: 10.1016/j.bmcl.2016.07.051. Epub 2016 Jul 27.

Abstract

Several p-terphenyl compounds have been isolated from the edible Chinese mushroom Thelephora vialis. Vialinin A, a p-terphenyl compound, strongly inhibits tumor necrosis factor-α production and release. Vialinin A inhibits the enzymatic activity of ubiquitin-specific peptidase 5, one of the target molecules in RBL-2H3 cells. Here we examined the inhibitory effect of p-terphenyl compounds, including vialinin A, against sentrin/SUMO-specific protease 1 (SENP1) enzymatic activity. The half maximal inhibitory concentration values of vialinin A and thelephantin G against full-length SENP1 were 1.64±0.23μM and 2.48±0.02μM, respectively. These findings suggest that p-terphenyl compounds are potent SENP1 inhibitors.

Keywords: SENP1; SUMO; TNF-α; Vialinin A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricales / chemistry
  • Agaricales / metabolism
  • Animals
  • Cell Line
  • Humans
  • Kinetics
  • Protein Binding
  • Rats
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • SUMO-1 Protein / antagonists & inhibitors
  • SUMO-1 Protein / metabolism*
  • Terphenyl Compounds / chemistry
  • Terphenyl Compounds / metabolism*
  • Tumor Necrosis Factor-alpha / antagonists & inhibitors
  • Tumor Necrosis Factor-alpha / metabolism*

Substances

  • Recombinant Proteins
  • SUMO-1 Protein
  • Terphenyl Compounds
  • Tumor Necrosis Factor-alpha
  • thelephantin G
  • vialinin A