Reflecting recent work in the Wennemers lab

Enzymes and peptide catalysts consist of the same building blocks but require vastly different environments to operate best. Published in Angewandte Chemie, Intl. Ed., researchers in the Wennemers lab show that an enzyme and a peptide catalyst can work together in a single reaction vessel to catalyze a two-step cascade reaction with high chemo- and stereoselectivity.

An enzyme and a peptide catalyze—in an aqueous buffer—a two-step cascade reaction with high chemo- and stereoselectivity in one pot. The optimization of the modular peptide catalyst and the identification of common reaction conditions were key for bringing the two worlds of enzyme and peptide catalysis together.

Abundant linear alcohols, nitroolefins, an alcohol oxidase, and a tripeptide catalyst provided chiral γ-nitroaldehydes in aqueous buffer. High yields, up to 92%, and stereoselectivities, up to 98%ee, were achieved for the cascade through the rational design of the peptide catalyst and the identification of common reaction conditions.

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