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Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone.


ABSTRACT: From the marine-derived fungus Penicillium sumatrense (Trichocomaceae), a pair of enantiomers [(+)-1 and (-)-1] were isolated with identical 1D NMR data to drazepinone, which was originally reported to have a trisubstituted naphthofuroazepinone skeleton. In this study, we confirmed the structures of the two enantiomers as drazepinone and revised their structures by detailed analysis of extensive 2D NMR data and a comparison of the calculated 13C chemical shifts, ECD, VCD, and ORD spectra with those of the experiment ones. (+)-1 and (-)-1 were evaluated for their PTP inhibitory activity in vitro. (-)-1 showed selective PTP inhibitory activity against PTP1B and TCPTP with IC50 values of 1.56 and 12.5 μg/mL, respectively.

SUBMITTER: Cao F 

PROVIDER: S-EPMC8708580 | biostudies-literature |

REPOSITORIES: biostudies-literature

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