Beauvericin is a cyclic depsipeptide mycotoxin produced by many filamentous fungi including Beauveria bassiana. It induces apoptosis through the induction of cytochrome c release and the activation of caspase 3. At sublethal concentrations beauvericin also inhibits angiogenesis and cell migration in vitro. These latter processes are important targets for cancer chemotherapy, thus beauvericin derivatives that show less toxicity might constitute interesting lead compounds for anticancer drug discovery. Beauvericin is biosynthesized by a nonribosomal peptide synthetase. This enzyme produces a dipeptide from D-hydroxyisovalerate (D-Hiv) and phenylalanine (Phe), N-methylates the Phe residue, and forms the cyclic triol. We have attempted the production of beauvericin derivatives by feeding hydroxyacid and amino acid substrate analogs of D-Hiv and Phe to Beauveria bassiana, and documented the incorporation of several of these analogs into novel beauvericins.