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Quantitative Affinity Screening of Macrocyclic Peptide Libraries Using Yeast Surface Display Technology.

Ylenia Mazzocato1,2, Zhanna Romanyuk1,2, Monica Chinellato1

  • 1Department of Molecular Sciences and Nanosystems, Ca' Foscari University of Venice, Mestre, Venice, Italy.

Methods in Molecular Biology (Clifton, N.J.)
|July 15, 2025
PubMed
Summary
This summary is machine-generated.

This study introduces a yeast surface display method for directed evolution of disulfide-tethered macrocyclic peptide ligands. This technique efficiently generates and isolates peptide ligands with desirable binding properties, streamlining drug discovery.

Keywords:
Cyclic peptideDirected evolutionDisulfide-tethered macrocyclic peptideDrug discoveryHigh-throughput screeningYeast surface display

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Drug Discovery

Background:

  • Directed evolution is a powerful tool for protein engineering.
  • Yeast surface display enables high-throughput screening of peptide libraries.
  • Macrocyclic peptides offer therapeutic potential but require efficient discovery methods.

Purpose of the Study:

  • To detail a protocol for in vitro-directed evolution of disulfide-tethered macrocyclic peptide ligands using yeast surface display.
  • To establish a method for rapid library generation and ligand selection.
  • To enable direct characterization of selected ligands on yeast cells.

Main Methods:

  • Generation of large combinatorial libraries of cysteine-rich peptides on yeast cell surface via homologous recombination.
  • Fluorescence-activated cell sorting (FACS) for rapid isolation of ligands with high binding affinity.
  • Direct quantitative characterization of yeast cell surface-displayed ligands, bypassing traditional synthesis and purification.

Main Results:

  • Successful generation of diverse peptide libraries displayed on yeast.
  • Efficient isolation of disulfide-tethered macrocyclic peptide ligands with favorable binding properties.
  • Demonstration of direct quantitative characterization of selected ligands on yeast, reducing experimental time and cost.

Conclusions:

  • Yeast surface display is an effective platform for the directed evolution of disulfide-tethered macrocyclic peptide ligands.
  • This protocol streamlines the discovery and characterization process, making it more efficient and cost-effective.
  • The method facilitates the identification of novel peptide ligands for therapeutic applications.