Miuraenamides, secondary metabolites of the marine myxobacterium Paraliomyxa miuraensis do not only show a high structural similarity to other cyclodepsipeptides isolated from sponges or terrestrial myxobacteria but they also exhibit a similar mode of action. They accelerate nucleation and polymerization of actin, and therefore interfere with cell division processes, at concentrations in the low nanomolar range. A late stage peptide modification allows the synthesis of a library of (simplified) miuraenamide derivatives with different halogenation and substitution pattern. Detailed SAR studies indicate, that bromination of the central tyrosine is essential for good biological activity, while the side chain of the C‐terminal amino acid can be varied or can even be removed.

Chelated ketone enolates are excellent nucleophiles for allylic alkylations. Electron‐withdrawing groups on the allyl moiety allow subsequent intramolecular Michael additions giving rise to piperidines with up to five stereogenic centers.