Journal
JOURNAL OF ANTIBIOTICS
Volume 53, Issue 2, Pages 105-109Publisher
JAPAN ANTIBIOT RES ASSN
DOI: 10.7164/antibiotics.53.105
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In our course of screening for novel proteasome inhibitors, TMC-95A and its diastereomers, TMC-95B to D, were isolated from the fermentation broth of Apiospora montagnei Sacc. TC 1093. TMC-95A inhibited the chymotrypsin-like (ChT-L), trypsin-like (TL), and peptidylglutamyl-peptide hydrolyzing (PGPH) activities of 20S proteasome with IC50 values of 5.4nM, 200 nM, and 60 nM, respectively. TMC-95B inhibited these activities to the same extent as TMC-95A, while the inhibitory activities of TMC-95C and D were 20 to 150 times weaker than that of TMC-95A and B. TMC-95A did not inhibit m-calpain, cathepsin L, and trypsin at 30 mu M, suggesting its high selectivity for proteasome. Taxonomy of the producing strain is also described.
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