85(P73) 藍藻Nostoc類より得られた酵素阻害物質の構造と活性(ポスター発表の部)
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In the continuous studies of enzyme inhibitors from cyanobacteria, we have found that Nostoc minutum (NIES-26) and N. linckia (NIES-25, 28) were a rich source of novel enzyme inhibitors. Here we report the isolation and structure elucidation of novel enzyme inhibitors form N. minutum and N. linckia. N. minutum (NIES-26) and N. linckia (NIES-25, 28) were obtained from the NIES-collection (Microbiol Culture Collection, the National Institute for Environmental Studies, Japan) and cultured in 10L glass bottles containing CB medium. The 80% methanol extracts of lyophilized cyanobacteria were subjected to solvent partitions, ODS column chromatography followed by ODS HPLC to yield nostopeptin-type peptides (1-10). Their structures were determined by FABMS and 2D NMR spectra. The absolute stereochemistries of usual and N-Me amino acids were determined to be all L-form by the HPLC analysis of the acid hydrolyzates derivatized with Marfey's reagent. 1, 2, 5, 6, and 8 inhibited elastase and chymotrypsin but 3, 4, and 7 had no elastase and chymotrypsin inhibitory activities. The 80% methanol extracts of lyophilized cyanobacteria [N. minutum (NIES-26) and N. linckia (NIES-25, 28)] were subjected to solvent partitions, ODS column chromatography followed by ODS HPLC to yield miutumamides A-D (12-15). Their structures were determined by FABMS and 2D NMR spectra. The absolute stereochemistries of usual amino acids were determined to be all L-form by the HPLC analysis of the acid hydrolyzates derivatized with Marfey's reagent. The absolute stereochemistries of Amopa and Hmp remains to be defined. 12-15 inhibited tyrosinase with the IC_<50> of 30μg/mL.
- 天然有機化合物討論会の論文
- 1998-08-31
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