118252-75-8

Upstream product

• 7801-71-0 N-benzyloxycarbonyl-L-leucyl-L-leucine 
• 116614-39-2 (3S)-3-<(N-benzyloxycarbonyl)-L-leucinyl>amino-1-diazo-5-methyl-2-hexanone 

Downstream Products

• 216489-70-2 (3S)-3-<(N-benzyloxycarbonyl)-L-leucinyl>amino-1-hydropxy-5-methyl-2-hexanone 

Relevant academic research and scientific papers

Nitrogen-containing 5-membered cyclic compounds and drugs containing these compounds as the active ingredient

An N-containing five-membered ring compound of formula (I) wherein all symbols are the same as described in the specification, and a non-toxic salt thereof. The compound of formula (I) has an inhibitory activity against cysteine protease and therefore it is useful as an agent for the prophylaxis and/or treatment of inflammatory diseases, diseases induced by apoptosis, diseases induced by disorders of immune responses, autoimmune diseases, diseases induced by decomposition of proteins which compose organism, shock, circulatory system disorders, blood coagulation systems disorders, malignant tumors, acquired immune deficiency syndrome (AIDS) and AIDS-related complex (ARC), parasitic diseases, nerve degeneration diseases, pulmonary disorders, bone resorption diseases, endocrinesthenia, etc.

Calpain inhibitors based on the quiescent affinity label concept: High rates of calpain inactivation with leaving groups derived from N-hydroxy peptide coupling reagents

A series of irreversible inhibitors of recombinant calpain has been synthesized and their rates of inactivation have been evaluated against calpain and cathepsin B, respectively. The design of the inhibitors was based on the quiescent affinity label concept. By choosing the appropriate affinity group and by employing leaving groups derived from N-hydroxy coupling reagents, good inhibitors of calpain with high rates of inactivation have been identified. However, poor aqueous stability limits their therapeutic utility. (C) 2000 Elsevier Science Ltd.

Potent dipeptidylketone inhibitors of the cysteine protease cathepsin K

Cathepsin K (EC 3.4.22.38) is a cysteine protease of the papain superfamily which is selectively expressed within the osteoclast. Several lines of evidence have pointed to the fact that this protease may play an important role in the degradation of the bone matrix. Potent and selective inhibitors of cathepsin K could be important therapeutic agents for the control of excessive bone resorption. Recently a series of peptide aldehydes have been shown to be potent inhibitors of cathepsin K. In an effort to design more selective and metabolically stable inhibitors of cathepsin K, a series of electronically attenuated alkoxymethylketones and thiomethylketones inhibitors have been synthesized. The X-ray co-crystal structure of one of these analogues in complex with cathepsin K shows the inhibitor binding in the primed side of the enzyme active site with a covalent interaction between the active site cysteine 25 and the carbonyl carbon of the inhibitor. Copyright (C) 1999 Elsevier Science Ltd.

Use of papain as a model for the structure-based design of cathepsin K inhibitors: Crystal structures of two papain-inhibitor complexes demonstrate binding to S'-subsites

Papain has been used as a surrogate enzyme in a drug design effort to obtain potent and selective inhibitors of cathepsin K, a new member of the papain superfamily of cysteine proteases that is selectively and highly expressed in osteoclasts and is implic