Linear and cyclic peptides from the entomopathogenic bacterium Xenorhabdus nematophilus

Three new peptides, xenortides A and B and xenematide, were isolated from a culture of the nematode-associated entomopathogenic bacterium Xenorhabdus nematophilus. Their structures were elucidated using NMR, MS, and chemical derivatization methods. Xenortides A and B are the N-phenethylamide and tryptamide derivatives, respectively, of the dipeptide (NMe-L-Leu-NMe-L-Phe). The cyclodepsipeptide xenematide has the sequence (Thr-Trp-Trp-Gly), with a 2-phenylacetamide substituent at the threonine residue and one D-tryptophan. The new peptides and the two known compounds xenocoumacin II and nematophin were tested for antibacterial, antifungal, insecticidal, and anti-Artemia salina activities. Xenematide and xenocoumacin II showed moderate antibacterial activities. Xenocoumacin II, nematophin, and the two xenortides were active in the Artemia salina assay, and xenematide acted weakly insecticidal.