PerspectivePeptide Synthesis

Catching up to nature's ribosomes

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Science  29 May 2020:
Vol. 368, Issue 6494, pp. 941
DOI: 10.1126/science.abb9711

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Summary

Chemical protein synthesis allows the systematic incorporation of one or more unnatural amino acids at precise locations along a protein backbone that enable structure-function relationship studies (1, 2). However, solid-phase peptide synthesis (SPPS) (3) is usually limited to peptides of 50 residues, and as a result, chemical protein synthesis requires native chemical ligation (NCL) (4) reactions for the chemoselective coupling of unprotected peptide fragments in solution. This combined multistep approach typically requires the synthesis and sequential ligation of at least three peptide fragments to access proteins, a process that remains relatively laborious. On page 980 of this issue, Hartrampf et al. (5) chemically synthesized single-domain proteins in hours. They circumvent the use of solution-phase chemistry by carefully optimizing iterative amino acid couplings on a solid support using a flow-chemistry setup (see the figure).

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