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Zusammenfassung:
A new cyclic peptide photoditritide (1), containing two rare amino acid D-homoarginine residues, was isolated from Photorhabdus temperata Meg1 after the nonribosomal peptide synthetase encoding gene pdtS was activated via promoter exchange. The structure of 1 was elucidated by HR-MS and NMR experiments. The absolute configurations of amino acids were determined according to the advanced Marfey's method after hydrolysis of 1. Bioactivity testing of 1 revealed potent antimicrobial activity against Micrococcus luteus with an MIC value of 3.0 mu M and weak antiprotozoal activity against Trypanosoma brucei rhodesiense with an IC50 value of 13 mu M. Additionally, the biosynthetic pathway of 1 was also proposed.
