cathepsin B Inhibitors

Cathepsin inhibitor peptide functions as a selective modulator of cathepsin B, engaging in specific interactions that disrupt the enzyme's active site. By mimicking substrate structures, it effectively competes for binding, leading to altered reaction kinetics and reduced proteolytic activity. This inhibition can induce conformational shifts in cathepsin B, influencing its stability and interaction with other cellular proteins, thereby playing a critical role in regulating proteolytic pathways.

S-Nitrosoglutathione (GSNO) serves as a potent modulator of cathepsin B activity through its unique nitrosylation mechanism. By forming S-nitrosothiol adducts, GSNO alters the redox state of the enzyme, impacting its catalytic efficiency and substrate specificity. This interaction can lead to conformational changes that affect enzyme stability and activity, highlighting the intricate balance of oxidative and nitrosative stress in cellular environments. The compound's role in post-translational modifications underscores its significance in proteolytic regulation.

Leupeptin hemisulfate acts as a potent inhibitor of cathepsin B by forming non-covalent interactions that stabilize the enzyme's inactive conformation. Its unique structure allows it to effectively mimic natural substrates, thereby blocking substrate access to the active site. This competitive inhibition alters the enzyme's catalytic efficiency and can lead to changes in the enzyme's tertiary structure, impacting its interactions with other proteases and cellular components.

ALLM, like ALLN, is another inhibitor targeting Cathepsin B, preventing its proteolytic function.

E-64-d is a selective inhibitor of cathepsin B, characterized by its ability to form covalent bonds with the enzyme's active site cysteine residue. This irreversible binding alters the enzyme's conformation, effectively preventing substrate hydrolysis. The compound's unique electrophilic nature enhances its reactivity, leading to a significant reduction in proteolytic activity. Additionally, E-64-d's specificity for cathepsin B over other cysteine proteases highlights its potential for targeted modulation of proteolytic pathways.

E-64 is a potent and irreversible inhibitor of cysteine proteases, including Cathepsin B, by interacting with its active site.

ALLN is a cell-permeable inhibitor that targets Cathepsin B, blocking its enzymatic activity.

MDL-28170 is a potent inhibitor of cathepsin B, distinguished by its ability to engage in specific non-covalent interactions with the enzyme's active site. This compound exhibits a unique binding affinity that stabilizes the enzyme in an inactive conformation, thereby disrupting its catalytic function. The kinetic profile of MDL-28170 reveals a rapid onset of inhibition, making it an effective tool for studying proteolytic mechanisms and enzyme regulation. Its selectivity for cathepsin B underscores its role in elucidating protease-related pathways.

K11777 is a potent inhibitor of Cathepsin B, disrupting its enzymatic function and potentially down-regulating its expression.

Z-FA-FMK is a fluoromethyl ketone-based irreversible inhibitor of Cathepsin B, preventing its proteolytic activity.