Abstract
A novel class of lipopeptides was isolated from Bacillus thuringiensis kurstaki HD-1. Four compounds (1-4) were separated by high-performance liquid chromatography and their primary structures determined using a combination of chemical reactions and mass spectrometry. The four lipopeptides were found to have the same amino acid sequence, Thr-Gly-Ala-Ser-His-Gln-Gln, but different fatty acids. The fatty acyl chain is linked to the N-terminal amino acid residue via an amide bond. Each lipopeptide has a lactone linkage between the carboxyl terminal amino acid and the hydroxyl group in the side chain of the serine residue. Antifungal activity was demonstrated against Stachybotrys charatum.
| Original language | English |
|---|---|
| Pages (from-to) | 1492-1496 |
| Number of pages | 5 |
| Journal | Journal of Natural Products |
| Volume | 63 |
| Issue number | 11 |
| DOIs | |
| State | Published - 2000 |
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