Lipohexin, a new inhibitor of prolyl endopeptidase from Moeszia lindtneri (HKI-0054) and Paecilomyces sp. (HKI-0055; HKI-0096). I. Screening, isolation and structure elucidation.

نویسندگان

  • S Heinze
  • M Ritzau
  • W Ihn
  • H Hülsmann
  • B Schlegel
  • K Dornberger
  • W F Fleck
  • M Zerlin
  • C Christner
  • U Gräfe
  • G Küllertz
  • G Fischer
چکیده

Lipohexin was isolated as a novel lipohexapeptide (I) (C39H68N6O9) from three fungal strains, Moeszia lindtneri HKI-0054, Paecilomyces sp. HKI-0055 and Paecilomyces sp. HKI-0096. The structure was elucidated by detailed mass spectrometric and NMR experiments. The proline-containing peptide displays moderate antibacterial activity against Bacillus subtilis ATCC 6633 and inhibits competitively the prolyl endopeptidase from human placenta.

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عنوان ژورنال:
  • The Journal of antibiotics

دوره 50 5  شماره 

صفحات  -

تاریخ انتشار 1997