biostudies-literatureKeuler TStudienstiftung des Deutschen VolkesDeutsche ForschungsgemeinschaftJ?rgen Manchot Stiftung8158-8162https://www.ebi.ac.uk/biostudies/studies/S-EPMC8908490biostudies-literatureUnknown7(9)In recent drug development efforts, particular emphasis has been devoted to the chemical interference with the NLRP3 inflammasome. A series of 12 tailored sulfonylureas was designed, prepared through convergent syntheses with a final sodium hydride-promoted reaction of isocyanates and sulfonamides, and subjected to a systematic, high-performance liquid chromatography-based survey of the chemical stability, a critical issue of sulfonylureas in terms of preparation, storage, and application. NLRP3 binding was determined by surface plasmon resonance spectroscopy. Sulfonylurea <b>2</b> was identified to be equipotent and similarly stable compared to the prototypical NLRP3 inhibitor MCC950.ACS omegaStructure-Stability Relationship of NLRP3 Inflammasome-Inhibiting Sulfonylureas.PMC8908490EXC2151 390873048Gutschow MKeuler TFerber DMarleaux MGeyer MfalseStructure-Stability Relationship of NLRP3 Inflammasome-Inhibiting Sulfonylureas.In recent drug development efforts, particular emphasis has been devoted to the chemical interference with the NLRP3 inflammasome. A series of 12 tailored sulfonylureas was designed, prepared through convergent syntheses with a final sodium hydride-promoted reaction of isocyanates and sulfonamides, and subjected to a systematic, high-performance liquid chromatography-based survey of the chemical stability, a critical issue of sulfonylureas in terms of preparation, storage, and application. NLRP3 binding was determined by surface plasmon resonance spectroscopy. Sulfonylurea <b>2</b> was identified to be equipotent and similarly stable compared to the prototypical NLRP3 inhibitor MCC950.2022-01-01T00:00:00Z2022 Mar2025-04-26T04:34:31.534Z2025-04-06T11:14:18.494ZS-EPMC89084903528473510.1021/acsomega.2c00125