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Isolation of Chemically Cyclized Peptide Binders Using Yeast Surface Display.

Kaitlyn Bacon1, Abigail Blain1, Matthew Burroughs1

  • 1Department of Chemical and Biomolecular Engineering, North Carolina State University, Box 7905, Engineering Building I, Raleigh, North Carolina 27695, United States.

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|August 14, 2020
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Summary

Researchers developed a novel yeast surface display method to efficiently isolate and characterize cyclic peptides with protein-binding capabilities for therapeutic applications. This technique bypasses the need for chemical synthesis, enabling rapid discovery of potent peptide binders.

Keywords:
affinity ligandscyclic peptidesinterleukin-17 (IL-17)library screeningyeast-display libraries

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Peptide Chemistry

Background:

  • Cyclic peptides engineered for protein binding are crucial for therapeutics and biotechnology.
  • Yeast surface display is a powerful platform for isolating and characterizing protein binders.

Purpose of the Study:

  • To develop and validate an efficient method for isolating and characterizing cyclic peptide binders using yeast surface display.
  • To demonstrate the isolation of cyclic peptide binders for both a model protein (lysozyme) and a therapeutic target (interleukin-17).

Main Methods:

  • Peptide cyclization via disuccinimidyl glutarate-mediated cross-linking of expressed linear peptides on yeast cell surface.
  • Screening of cyclic heptapeptide libraries using magnetic selection and fluorescence-activated cell sorting (FACS).
  • Quantitative affinity estimation directly from yeast surface-displayed cyclic peptides, avoiding chemical synthesis.

Main Results:

  • Isolated cyclic heptapeptide binders for lysozyme with low micromolar affinity (KD ~ 1.2-3.7 μM), demonstrating selective and cyclization-dependent binding.
  • Successfully isolated cyclic heptapeptides targeting human interleukin-17 (IL-17) with moderate apparent affinity (KD ~ 300 nM).
  • Validated yeast surface display as an efficient platform for both isolation and affinity characterization of chemically modified cyclic peptides.

Conclusions:

  • Yeast surface display provides an efficient and versatile platform for the discovery and characterization of cyclic peptide binders.
  • The developed method enables rapid isolation of peptides with therapeutic potential, bypassing traditional chemical synthesis steps.
  • This approach broadens the scope of cyclic peptide engineering for diverse biotechnological and therapeutic applications.