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Electrifying Peptide Synthesis for Directed Evolution of Artificial Enzymes

Project description

Novel electrochemical peptide synthesis platforms will lead to robust artificial-enzyme catalysts

In the temperate internal environments of living organisms, nature’s catalysts (delicate protein enzymes) convert small molecules into others for a variety of cellular metabolic functions. Many of these reactions are relevant to energy, and harnessing them to support conversion processes for the renewable energy transition would provide a sustainable alternative to current rare precious metals. However, the functioning of these delicate enzymes is impaired under the extreme operating conditions of fuel cells or electrolysers. The EU-funded E-VOLUTION project will use directed evolution methods already established for natural amino acids and biological conditions to make highly active and robust artificial enzymes from natural and artificial amino acids.

Objective

Global climate and energy challenges require efficient, robust and scalable catalysts for the conversion of renewable energies. Nature has evolved extremely active catalysts (enzymes) for the conversion of small molecules relevant to energy (H2, CO2, N2). The scalability of these enzymes offers distinct advantages over the rare, precious metals that are currently used in energy conversion. Unfortunately, the enzymes are unable to tolerate the extreme conditions of operating fuel cells or electrolyzers. Directed evolution is a powerful approach for improving enzymes, but is mostly restricted to natural amino acids and biological conditions, with limited compatibility for evolving enzymes toward enhanced resistance in abiotic systems. Here, I aim to establish directed evolution in fully abiotic systems, using artificial amino acids to make artificial enzymes that are stable even in extreme conditions. Towards this, I will establish new electrochemical peptide synthesis platforms to enable the generation of enzyme-length peptides using both natural and artificial amino acids. Extended libraries of artificial enzyme variants will be produced and screened directly on electrode microarrays. Top enzyme candidates for the conversion of H2 will be selected using fuel cell/electrolyzer conditions as the evolutionary criteria. By the end, I will have a new procedure for synthesizing libraries of full-length artificial proteins, enabling the creation of thousands of enzyme variants using artificial building blocks. The generation of high-quality datasets will be transformative to drive future machine learning-based evolution steps for both full size enzymes and small-molecule catalysts with applications beyond H2 evolution. We will have discovered highly active catalysts able to sustain conditions of large-scale energy conversion devices, accelerating breakthroughs toward the economically competitive use of renewable energies for fuel and chemical production.

Host institution

TECHNISCHE UNIVERSITAET MUENCHEN
Net EU contribution
€ 1 997 993,00
Address
Arcisstrasse 21
80333 Muenchen
Germany

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Region
Bayern Oberbayern München, Kreisfreie Stadt
Activity type
Higher or Secondary Education Establishments
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Total cost
€ 1 997 993,00

Beneficiaries (1)