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Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity
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Phage-displayed macrocyclic glycopeptide libraries.

Simon Ng1, Ratmir Derda1

  • 1Alberta Glycomics Centre and Department of Chemistry, University of Alberta, Edmonton, AB T6G 2G2, Canada. ratmir@ualberta.ca.

Organic & Biomolecular Chemistry
|February 19, 2016
PubMed
Summary
This summary is machine-generated.

This study presents a novel method for creating macrocyclic glycopeptide libraries efficiently. The technique uses phage-displayed peptides and dichloro-oxime derivatives, enabling genetic selection for glycan-binding proteins.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Chemistry

Background:

  • Macrocyclic glycopeptides are important in biological processes.
  • Generating diverse libraries of these molecules is challenging.
  • Phage display is a powerful tool for molecular selection.

Purpose of the Study:

  • To develop an efficient one-step method for generating libraries of macrocyclic glycopeptides.
  • To demonstrate the compatibility of the method with phage display technology.
  • To enable genetic selection of macrocyclic glycopeptides for specific glycan-binding proteins.

Main Methods:

  • Reaction of phage-displayed peptide libraries with dichloro-oxime derivatives.
  • Assessment of phage replication and viability post-reaction.
  • Evaluation of reaction site-selectivity on phage particles.

Main Results:

  • An efficient one-step method for generating macrocyclic glycopeptide libraries was established.
  • The chemical reactions did not impede phage replication in bacteria.
  • The reactions were site-selective for phage-displayed peptides, leaving other phage proteins unmodified.

Conclusions:

  • The described technology provides an efficient route to macrocyclic glycopeptide libraries.
  • This method is compatible with phage display and bacterial replication.
  • The approach will be instrumental in the genetic selection of macrocyclic glycopeptides targeting glycan-binding proteins.