Taxonomy, Production, Isolation, and Biological Activities
نویسندگان
چکیده
In our course of screening for novel proteasome inhibitors, TMC-95A and its diastereomers, TMC-95Bto D, were isolated from the fermentation broth of Apiospora montagnei Sacc. TC 1093. TMC-95Ainhibited the chymotrypsin-like (ChT-L), trypsin-like (TL), and peptidylglutamyl-peptide hydrolyzing (PGPH) activities of 20S proteasome with IC50 values of 5.4nM, 200nM, and 60nM, respectively. TMC-95Binhibited these activities to the same extent as TMC-95A, while the inhibitory activities of TMC-95Cand D were 20 to 150 times weaker than that of TMC-95Aand B. TMC-95Adid not inhibit m-calpain, cathepsin L, and trypsin at 30 jiu, suggesting its high selectivity for proteasome. Taxonomyof the producing strain is also described.
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