caspase-2 Inhibitors

Z-FA-FMK is a selective inhibitor of caspase-2, characterized by its ability to form covalent bonds with the active site cysteine residue. This irreversible binding alters the enzyme's conformation, effectively blocking its proteolytic activity. The compound's unique structure allows for specific interactions with the caspase-2 active site, influencing apoptotic signaling pathways. Its stability in various environments enhances its potential to dissect cellular mechanisms involving caspase-2 regulation.

Caspase-2 inhibitor is characterized by its selective binding affinity for the caspase-2 enzyme, disrupting its catalytic activity through unique molecular interactions. This compound exhibits a distinctive mechanism of action, where it stabilizes an inactive conformation of the enzyme, effectively blocking substrate access. Its reaction kinetics indicate a competitive inhibition pattern, allowing for detailed exploration of caspase-2's role in cellular processes and apoptotic signaling pathways.

Caspase Inhibitor, Negative Control, functions as a potent modulator of caspase-2 activity, exhibiting a unique ability to alter enzyme conformation. By engaging in specific non-covalent interactions, it prevents the formation of the active site, thereby hindering substrate binding. This inhibitor showcases distinct reaction kinetics, revealing insights into the regulatory mechanisms of apoptosis and cellular signaling. Its behavior highlights the intricate balance of proteolytic pathways in cellular homeostasis.

VAD-fmk is a pan-caspase inhibitor, but it can also inhibit caspase-2 when used at specific concentrations.

C2-8 is a selective and reversible caspase-2 inhibitor that has been studied for its potential therapeutic applications in neurodegenerative diseases.