Xenortide
Xenortide A
Xenortide B
Xenortide C
Xenortide D
Chemical structure of xenortides
The xenortides (A-D) are a class of linear peptides isolated from the bacterium sleeping sickness) and Plasmodium falciparum (malaria), however it is also the most toxic to mammalian cells which limits its viability as a treatment.[1]
The biosynthesis of xenortides A-D consists of two
thiolation domain, and has been implicated for the loading of N-methylleucine (xenortides A-B) or N-methylvaline (xenortides C-D). The second NRPS (XndB) consists of a condensation, adenylation, methylation, thiolation, and terminal condensation domains. XndB has been implicated in elongation with N-methylphenylalanine, as well as the final condensation of the enzyme-bound peptide with either decarboxylated phenylalanine (xenortides A and C) or decarboxylated tryptophan (xenortides B and D), ending the biosynthesis.[1]
