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.

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.

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / isolation & purification*
  • Anti-Bacterial Agents / pharmacology*
  • Bacillus subtilis / drug effects
  • Humans
  • Lipoproteins / chemistry
  • Lipoproteins / isolation & purification*
  • Lipoproteins / pharmacology*
  • Microbial Sensitivity Tests
  • Mitosporic Fungi / metabolism
  • Molecular Structure
  • Paecilomyces / metabolism
  • Peptides*
  • Prolyl Oligopeptidases
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / chemistry
  • Serine Proteinase Inhibitors / isolation & purification*
  • Serine Proteinase Inhibitors / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Lipoproteins
  • Peptides
  • Serine Proteinase Inhibitors
  • lipohexin
  • Serine Endopeptidases
  • PREPL protein, human
  • Prolyl Oligopeptidases