3 results match your criteria: "Kansas University Specialized Chemistry Center[Affiliation]"
Phenylsulfamoyl Benzoic Acid Inhibitor of ERAP2 with a Novel Mode of Inhibition.
ACS Chem Biol
July 2022
Department of Pathology, University of Massachusetts Chan Medical School, Worcester, Massachusetts 01655, United States.
Article Synopsis
- ERAP1 and ERAP2 are important enzymes involved in peptide processing for immune responses, making them targets for cancer and autoimmune disorder treatments.
- The study identifies a new compound that inhibits ERAP2 and describes its distinct binding site and uncompetitive mechanism, while also revealing that the same compound activates ERAP1's hydrolysis process.
- Key residue changes in ERAP1 and ERAP2 influence how these compounds bind, suggesting potential paths for developing more effective and targeted inhibitors.
Discovery of Selective Inhibitors of Endoplasmic Reticulum Aminopeptidase 1.
J Med Chem
January 2020
Kansas University Specialized Chemistry Center, Lawrence , Kansas 66047 , United States.
ERAP1 is an endoplasmic reticulum-resident zinc aminopeptidase that plays an important role in the immune system by trimming peptides for loading onto major histocompatibility complex proteins. Here, we report discovery of the first inhibitors selective for ERAP1 over its paralogues ERAP2 and IRAP. Compound (-(-(2-(1-indol-3-yl)ethyl)carbamimidoyl)-2,5-difluorobenzenesulfonamide) and compound (1-(1-(4-acetylpiperazine-1-carbonyl)cyclohexyl)-3-(-tolyl)urea) are competitive inhibitors of ERAP1 aminopeptidase activity.
View Article and Find Full Text PDF