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 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.
Heinze
S
S
Hans-Knöll-Institute of Natural Products Research, Jena, Germany.
Ritzau
M
M
Ihn
W
W
Hülsmann
H
H
Schlegel
B
B
Dornberger
K
K
Fleck
W F
WF
Zerlin
M
M
Christner
C
C
Gräfe
U
U
Küllertz
G
G
Fischer
G
G
D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D001412:Bacillus subtilis / Q000187:drug effects; D006801:Humans; D008074:Lipoproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D008826:Microbial Sensitivity Tests; D003904:Mitosporic Fungi / Q000378:metabolism; D015394:Molecular Structure; D010143:Paecilomyces / Q000378:metabolism; D010455:Peptides; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D008074:Lipoproteins; D010455:Peptides; D015842:Serine Proteinase Inhibitors; C107025:lipohexin; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases