Lipohexin, a New Inhibitor of Prolyl Endopeptidase from Moeszia lindtneri (HKI-0054) and Paedlomyces sp. (HKI-0055; HKI-0096) II. Inhibitory Activities and Specificity

CLAUDIA CHRISTNER; MARION ZERLIN; UDO GRÄFE; STEPHAN HEINZE; GERHARD KÜLLERTZ; GUNTER FISCHER

doi:10.7164/antibiotics.50.384

Lipohexin, a New Inhibitor of Prolyl Endopeptidase from Moeszia lindtneri (HKI-0054) and Paedlomyces sp. (HKI-0055; HKI-0096)

II. Inhibitory Activities and Specificity

CLAUDIA CHRISTNER, MARION ZERLIN, UDO GRÄFE, STEPHAN HEINZE, GERHARD KÜLLERTZ, GUNTER FISCHER

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JOURNAL FREE ACCESS

1997 Volume 50 Issue 5 Pages 384-389

DOI https://doi.org/10.7164/antibiotics.50.384

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Abstract

The new proline-containing lipohexapeptide lipohexin (I) isolated from three fungal strains, Moeszia lindtneri (HKI-0054) and Paedlomyces sp. (HKI-0055 and HKI-0096) is a competitive inhibitor of prolyl endopeptidase (PEP) from human placenta with IC₅₀ of 3.5 μM. Specificity of lipohexin (I) is indicated by the much weaker inhibitory activity against bacterial prolyl endopeptidase from Flavobacterium meningosepticum (IC₅₀ 25 μM). No effect of lipohexin (I) was found on the activity of mechanistically related proteases such as proline specific proteases and other serine proteases.

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