Discovery and Development of NLRP3 Inhibitors Targeting the LRR Domain to Disrupt NLRP3-NEK7 Interaction for the Treatment of Rheumatoid Arthritis.
Bing-Yan LiPei LiLin-Yin WeiJia ZouYu-Hang WangQi-Dong YouCheng JiangBin DiLi-Li XuPublished in: Journal of medicinal chemistry (2024)
Rheumatoid arthritis (RA) is a chronic autoimmune disease. Targeting NLRP3 inflammasome, specifically its interaction with NEK7 via the LRR domain of NLRP3, is a promising therapeutic strategy. Our research aimed to disrupt this interaction by focusing on the LRR domain. Through virtual screening, we identified five compounds with potent anti-inflammatory effects and ideal LRR binding affinity. Lead compound C878-1943 underwent structural optimization, yielding pyridoimidazole derivatives with different anti-inflammatory activities. Compound I-19 from the initial series effectively inhibited caspase-1 and IL-1β release in an adjuvant-induced arthritis (AIA) rat model, significantly reducing joint swelling and spleen/thymus indices. To further enhance potency and extend in vivo half-life, a second series including II-8 was developed, demonstrating superior efficacy and longer half-life. Both I-19 and II-8 bind to the LRR domain, inhibiting NLRP3 inflammasome activation. These findings introduce novel small molecule inhibitors targeting the LRR domain of NLRP3 protein and disrupt NLRP3-NEK7 interaction, offering a novel approach for RA treatment.
Keyphrases
- nlrp inflammasome
- rheumatoid arthritis
- small molecule
- disease activity
- anti inflammatory
- cancer therapy
- ankylosing spondylitis
- protein protein
- early stage
- systemic lupus erythematosus
- cell death
- signaling pathway
- multiple sclerosis
- drug induced
- high throughput
- oxidative stress
- mass spectrometry
- diabetic rats
- drug delivery
- transcription factor
- high glucose
- replacement therapy
- binding protein
- smoking cessation
- capillary electrophoresis