Phototemtide A, a Cyclic Lipopeptide Heterologously Expressed from Photorhabdus temperata Meg1, Shows Selective Antiprotozoal Activity.
Lei ZhaoTien Duy VoMarcel KaiserHelge B BodePublished in: Chembiochem : a European journal of chemical biology (2020)
A new cyclic lipopeptide, phototemtide A (1), was isolated from Escherichia coli expressing the biosynthetic gene cluster pttABC from Photorhabdus temperata Meg1. The structure of 1 was elucidated by HR-ESI-MS and NMR experiments. The absolute configurations of amino acids and 3-hydroxyoctanoic acid in 1 were determined by using the advanced Marfey's method and comparison after total synthesis of 1, respectively. Additionally, three new minor derivatives, phototemtides B-D (2-4), were identified by detailed HPLC-MS analysis. Phototemtide A (1) showed weak antiprotozoal activity against Plasmodium falciparum, with an IC50 value of 9.8 μm. The biosynthesis of phototemtides A-D (1-4) was also proposed.
Keyphrases
- ms ms
- plasmodium falciparum
- mass spectrometry
- escherichia coli
- multiple sclerosis
- amino acid
- magnetic resonance
- high resolution
- genome wide
- high performance liquid chromatography
- resting state
- gene expression
- simultaneous determination
- copy number
- dna methylation
- liquid chromatography
- functional connectivity
- klebsiella pneumoniae
- tandem mass spectrometry
- solid phase extraction
- cell wall