Activation of a C-H bond of complex molecules surpasses the need of de novo synthesis. This late-stage functionalization, if selective, enables modifications and installation of chemical handles on compounds. This approach can lead to the facile development of therapeutics as well as applications in industry-related fields. Aromatic prenyltransferase (ArPT) enzymes are ubiquitous in all walks of life. ArPTs are encoded in many biosynthetic gene clusters of natural products and are involved in the decoration of these molecules with different prenyl groups. They catalyze the transfer of prenyl moieties from pyrophosphate donors to aromatic acceptor substrates. ArPTs have relaxed substrate specificities allowing them to accept nonnative acceptor and donors and can thus be used to catalyze nonnatural reactions. Our lab has developed a high-throughput chemoenzymatic platform of wildtype and engineered ArPTs and in house synthesized pyrophosphate donors. This platform has enabled us facilitate the late-stage functionalization of several aromatic-containing compounds and tryptophan-containing peptides in a selective manner. This approach has led our lab to modify and tag biologically active peptides and compounds.

Functionalization of tryptophan-containing peptides using biocatalysis

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