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Directed Evolution of Glycopeptides Using mRNA Display.

Satoru Horiya1, Jennifer K Bailey1, Isaac J Krauss1

  • 1Brandeis University, Waltham, MA, United States.

Methods in Enzymology
|September 23, 2017
PubMed
Summary

Directed evolution can now create diverse glycopeptide libraries for drug discovery. This new method enables selection of glycopeptides with specific binding properties for therapeutic applications.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Directed evolution is crucial for discovering novel peptides and proteins with specific functions.
  • Glycosylation is abundant and vital in nature, making glycopeptide and glycoprotein evolution highly desirable.
  • Current directed evolution platforms face limitations in controlling glycan structure and homogeneity.

Purpose of the Study:

  • To present an optimized protocol for directed evolution of glycopeptide libraries.
  • To enable the creation of large-scale glycopeptide libraries (~10^13 sequences) for target selection.
  • To demonstrate the method's applicability using the HIV broadly neutralizing antibody 2G12 as a target.

Main Methods:

  • Combines in vitro peptide selection via mRNA display.
Keywords:
2G12Broadly neutralizing antibodiesClick chemistryCuAACDirected evolutionGlycopeptide/glycoproteinHIVMultivalencySelectionmRNA display

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  • Incorporates unnatural amino acid incorporation.
  • Utilizes chemical attachment of synthetic oligosaccharides.

    • Main Results:

    • Successfully created and selected glycopeptide libraries with ~10^13 sequences.
    • Demonstrated selection against the HIV antibody 2G12, which targets specific glycan structures.
    • The method allows for the decoration of glycopeptides with virtually any desired glycan.

    Conclusions:

    • The developed method offers a powerful platform for directed evolution of glycopeptides.
    • This approach overcomes limitations of existing methods for glycopeptide and glycoprotein engineering.
    • The protocol is adaptable for diverse glycans and targets in glycobiology research and therapeutic development.