Keap1-Kelch-targeting protein-protein interaction inhibitors, but not reversibly-binding electrophiles, increase the thermostability of Keap1 in the cellular environment

Key Points

• To investigate how different inhibitors affect the thermostability of Keap1 in a cellular context.
• Evaluated protein-protein interactions using inhibitors targeting Keap1-Kelch.
• Assessed the impact of electrophiles on Keap1 stability.
• Conducted stability assays under various cellular conditions.
• Keap1 thermostability increased significantly with protein-protein interaction inhibitors.
• Reversibly-binding electrophiles did not enhance Keap1 stability.
• Enhanced stability correlates with improved cellular defense against stress.