Universal peptide synthesis via solid-phase methods fused with chemputation

Jacopo Zero, Tristan J. Tyler and Leroy Cronin ()
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Jacopo Zero: University of Glasgow, University Avenue
Tristan J. Tyler: University of Glasgow, University Avenue
Leroy Cronin: University of Glasgow, University Avenue

Nature Communications, 2025, vol. 16, issue 1, 1-11

Abstract: Abstract Since the advent of automated solid-phase peptide synthesis (SPPS), many commercial platforms have been developed, facilitating cutting-edge research across many biochemical fields. However, despite considerable technological advancements, these systems remain limited in flexibility and chemical capability. Herein, we present a fully automated programmable platform that combines the efficiency of SPPS with the chemical flexibility of a Chemical Processing Unit (Chemputer). SPPS protocols, from resin swelling to peptide precipitation, are captured and automated using the Chemical Description Language (χDL), affording peptide sequences in high purity (>79%) and on a multi-milligram scale. Owing to the modularity of the platform, valuable transformations are integrated into the workflow, including ring-closing metathesis, copper-catalyzed azide-alkyne cycloaddition, and native chemical ligation. These tailored modifications are carried out in one, uninterrupted synthetic protocol, performing up to 1635-unit operations, executed over 85 h of activity, producing peptides such as GHRH(1-29), Semaglutide, and Capitellacin, finally unlocking bottlenecks in automated SPPS.

Date: 2025
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DOI: 10.1038/s41467-025-62344-2

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