leupeptin

Leupeptin is a naturally occurring tripeptide protease inhibitor produced by actinomycetes such as Streptomyces species[3][7]. It inhibits serine, cysteine, and threonine proteases—including trypsin, plasmin, calpain, papain, and cathepsins B, H and L—by acting as a reversible competitive inhibitor that covalently binds to the catalytic sites of these enzymes[4][5][6]. Leupeptin does not inhibit α-chymotrypsin or thrombin. It is widely used in biochemical research to prevent protein degradation during cell lysis and extraction procedures. In preclinical studies it has shown neuroprotective effects (e.g., protecting motor neurons from apoptosis), potential for enhancing muscle function after nerve injury[5], prevention of muscular dystrophy in animal models[6], and protection against hearing loss caused by acoustic trauma or ototoxic drugs[7]. Leupeptin can also inhibit certain viral proteases (e.g., human coronavirus 229E)[6][8].

Other names

N-acetyl-L-leucyl-L-leucyl-L-argininalacetyl-leucyl-leucyl-argininalacetyl-l-leucyl-l-leucyl-l-argininalAcetyl-Leu-Leu-Arg-alLeupeptins