Cathepsin Inhibitors

H-Leu-Phe-OH acts as a selective inhibitor of cathepsins, showcasing a unique ability to modulate enzyme activity through its specific amino acid sequence. The compound engages in non-covalent interactions, stabilizing the enzyme-inhibitor complex and altering the catalytic pathway. Its structural features facilitate competitive inhibition, providing insights into the dynamics of proteolytic regulation. This behavior underscores its role in elucidating enzyme kinetics and specificity in proteolytic pathways.

Z-Phe-Tyr(tBu)-diazomethylketone serves as a potent cathepsin inhibitor, characterized by its unique diazomethylketone moiety that enables covalent modification of the active site. This compound exhibits a high affinity for the enzyme, leading to irreversible inhibition. Its bulky t-butyl group enhances selectivity, while the aromatic residues contribute to π-π stacking interactions, influencing binding dynamics. The compound's reactivity profile provides valuable insights into enzyme regulation mechanisms and specificity.