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  3. Ribosomal Translation And Display Selection Of Cyclic Glycopeptides Through Genetic Reprogramming.
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  3. Ribosomal Translation And Display Selection Of Cyclic Glycopeptides Through Genetic Reprogramming.

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Ribosomal Translation and Display Selection of Cyclic Glycopeptides through Genetic Reprogramming.

Jason Johansen-Leete1,2, Yichen Zhong1,2, Beiyuan Cui1,2

  • 1School of Chemistry, The University of Sydney, Sydney NSW 2006, Australia.

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|March 4, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

Researchers developed a novel method for incorporating glycosyl-amino acids into proteins using flexizyme-mediated genetic reprogramming. This enables the discovery of new glycopeptide drugs with antiplatelet and lysosome trafficking activities.

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Drug Discovery

Background:

  • Ribosomal protein synthesis is limited in incorporating non-natural amino acids.
  • Genetic reprogramming offers a potential solution for expanding the protein synthesis toolbox.

Purpose of the Study:

  • To develop a robust method for ribosomal incorporation of glycosyl-amino acids.
  • To apply this method for the discovery of novel glycopeptide-based therapeutics.

Main Methods:

  • Flexizyme-mediated reprogramming of initiating AUG codons with glycosyl-dipeptides.
  • In vitro mRNA display for de novo library selection.
  • Characterization of identified glycopeptides for biological activity.

Main Results:

  • Successful ribosomal incorporation of glycosyl-amino acids.
  • Discovery of α-l-fucosylated cyclic peptides inhibiting P-selectin with antiplatelet activity.
  • Discovery of β-d-N-acetylgalactosamine-containing cyclic glycopeptides activating ASGPR for lysosome trafficking.

Conclusions:

  • The developed method is a powerful platform for de novo glycopeptide ligand discovery.
  • This expands genetic reprogramming capabilities for large, complex modifications in ribosomal translation.