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.
Affiliations
- 1. Department of Nutritional Science and Food Safety, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka Setagaya-ku, Tokyo 156-8502, Japan; Organization of Advanced Science and Technology, Kobe University, Kobe, Hyogo 657-8501, Japan.
- 2. Department of Nutritional Science and Food Safety, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka Setagaya-ku, Tokyo 156-8502, Japan.
- 3. Organization of Advanced Science and Technology, Kobe University, Kobe, Hyogo 657-8501, Japan; Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Kobe, Hyogo 651-8501, Japan.
- 4. Department of Nutritional Science and Food Safety, Faculty of Applied Bioscience, Tokyo University of Agriculture, 1-1-1 Sakuragaoka Setagaya-ku, Tokyo 156-8502, Japan. Electronic address: [email protected].
PMID: 27491710
DOI: 10.1016/j.bmcl.2016.07.051
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.