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Updated: May 15, 2026
12:36
A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits
Published on: February 16, 2014
Phage selection of bicyclic peptides
Inmaculada Rentero Rebollo1, Christian Heinis
1Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Methods (San Diego, Calif.)
|January 15, 2013
Summary
Bicyclic peptides offer advantages over larger proteins for drug development. This study details protocols for using phage display to isolate high-affinity bicyclic peptide ligands for protein targets.
Area of Science:
- Biochemistry
- Molecular Biology
- Drug Discovery
Background:
- Bicyclic peptides are small, constrained peptides with high affinity and selectivity for protein targets.
- Their size offers advantages like chemical synthesis, improved tissue penetration, and diverse application routes compared to larger protein ligands.
Purpose of the Study:
- To provide detailed, step-by-step protocols for isolating bicyclic peptide ligands using phage display technology.
- To enable researchers to generate high-affinity binders for various protein targets.
Main Methods:
- Phage display library generation.
- Affinity selection processes.
- Ligand characterization techniques.
Main Results:
- Successful isolation of high-affinity bicyclic peptide ligands for diverse protein targets.
- Established protocols applicable in laboratory settings.
Conclusions:
- Phage display is an effective and cost-efficient method for identifying bicyclic peptide ligands.
- The provided protocols facilitate the generation of potent peptide-based therapeutics.
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