LIPOHEXIN, A NEW INHIBITOR OF PROLYL ENDOPEPTIDASE FROM MOESZIA-LINDTNERI (HKI-0054) AND PAECILOMYCES SP (HKI-0055, HKI-0096) .1. SCREENING, ISOLATION AND STRUCTURE ELUCIDATION

Authors
HEINZE S RITZAU M IHN W HULSMANN H SCHLEGEL B DORNBERGER K FLECK WF ZERLIN M CHRISTNER C GRAFE U KULLERTZ G FISCHER G
Citation
S. Heinze et al., LIPOHEXIN, A NEW INHIBITOR OF PROLYL ENDOPEPTIDASE FROM MOESZIA-LINDTNERI (HKI-0054) AND PAECILOMYCES SP (HKI-0055, HKI-0096) .1. SCREENING, ISOLATION AND STRUCTURE ELUCIDATION, Journal of antibiotics, 50(5), 1997, pp. 379-383
Citations number
16
Categorie Soggetti
Pharmacology & Pharmacy",Immunology,"Biothechnology & Applied Migrobiology
Journal title
Journal of antibiotics → ACNP
ISSN journal
00218820
Volume
50
Issue
5
Year of publication
1997
Pages
379 - 383
Database
ISI
SICI code
0021-8820(1997)50:5<379:LANIOP>2.0.ZU;2-H
Abstract
Lipohexin was isolated as a novel lipohexapeptide (I) (C39H68N6O9) fro m three fungal strains, Moeszia lindtneri HKI-0054, Paecilomyces sp. H KI-0055 and Paecilomyces sp. HKI-0096. The structure was elucidated by detailed mass spectrometric and NMR experiments. The proline-containi ng peptide displays moderate antibacterial activity against Bacillus s ubtilis ATCC 6633 and inhibits competitively the prolyl endopeptidase from human placenta.