期刊
BIOLOGICAL CHEMISTRY
卷 384, 期 12, 页码 1613-1618出版社
WALTER DE GRUYTER & CO
DOI: 10.1515/BC.2003.179
关键词
Aza-asparagine; clan CD enzymes; cysteine proteases; epoxysuccinate; irreversible inhibitor; synthetic inhibitor
资金
- NIAID NIH HHS [AI053247] Funding Source: Medline
- NIGMS NIH HHS [GM61964, GM54401] Funding Source: Medline
Azapeptide epoxides are a new class of irreversible cysteine protease inhibitors. Derivatives containing a P1 azaasparagine residue are specific for Schistosoma mansoni and pig kidney legumains, which are clan CD cysteine proteases. The inhibitors have secondorder rate constants of up to 10(4) M(-1)s(-1) with pig kidney legumain and IC50 values as low as 45 nM with S. mansoni legumain. The most potent epoxides contain an ester moiety with S,S stereochemistry attached to the epoxide. Interestingly, amide and amino acid derivatives of the epoxysuccinate moiety were not inhibitors of legumain, while disubstituted amide derivatives are quite potent. The inhibitors have little or no inhibitory activity with other proteases such as caspases, chymotrypsin, papain, cathepsin B, granzyme B, and various aspartyl proteases.
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