2. Academic Validation
  3. 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

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

  • J Antibiot (Tokyo). 1997 May;50(5):379-83. doi: 10.7164/antibiotics.50.379.
S Heinze 1,  M Ritzau,  W Ihn,  H Hülsmann,  B Schlegel,  K Dornberger,  W F Fleck,  M Zerlin,  C Christner,  U Gräfe,  G Küllertz,  G Fischer
Affiliations

Affiliation

  • 1 Hans-Knöll-Institute of Natural Products Research, Jena, Germany.
PMID: 9207906 DOI: 10.7164/antibiotics.50.379
Abstract

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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