Phage selection of bicyclic peptides
Open accessAbstract
Bicyclic peptides are small, constrained peptides that can bind with high affinity and selectivity to protein targets. Their small size provides a number of advantages over larger protein-based ligands, including access to chemical synthesis, better tissue penetration, and a wider choice of application routes. Bicyclic peptide ligands can be identified using phage display technology with moderate effort and cost. Here we provide step-by-step protocols for the isolation of bicyclic peptide ligands using phage display. These protocols have been successfully used in our laboratory for the generation of high-affinity binders to a variety of protein targets. We describe library generation, affinity selection and ligand characterization, and provide troubleshooting advice concerning frequent problems.
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Structure–Affinity Relationship Analysis and Affinity Maturation of a Calprotectin‐Binding Peptide
Soler, L. F., Hu, C., Ricken, B., Díaz‐Perlas, C., Gerhold, C., & Heinis, C. (2025) · ChemBioChem · doi:10.1002/cbic.202500071
Self-citationLate-stage peptide nitroarylation: stereoelectronic tuning and molecular recognition
Cain, J. M., Dowling, M., DiGiorno, M. C., Banaszek, A., & Sawyer, N. (2026) · Organic & Biomolecular Chemistry · doi:10.1039/d6ob00394j
Zhang, Y., Vinogradov, A. A., Hamada, K., Sun, Y., Sengoku, T., & Suga, H. (2026) · Angewandte Chemie · doi:10.1002/ange.2417165
Phage Display-Derived Cyclic Peptides as Ligand-Specific Modulators for β 2 -Integrin ReceptorsPreprint
Plüss, C. J., Vogt, S. A., Ciullo, L., Mancuso, R. V., Goetze-Ebert, T., Kehr, L., Ricklin, D., & Lamers, C. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.12.744392
- Authors
- Rentero Rebollo, I., & Heinis, C.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Corresponding author
- Heinis, Christian
- ORCID
- Heinis, Christian
- Venue
- Methods
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 60
- Issue
- 1
- Pages
- 46-54
- ISSN
- 1046-2023 (ISSN-L)
- OpenAlex
- W2071135907
- Cited by
- 80
- References
- 30
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 2 · 2023: 7 · 2022: 4 · 2021: 7 · 2020: 15 · 2019: 2 · 2018: 7 · 2017: 7 · 2016: 2 · 2015: 3 · 2014: 8 · 2013: 4
- FWCI
- 0.56
- Type
- journal article
- Language
- en
- Open access
- green
- infoscience.epfl.ch
- Locations
- Methods (publishedVersion)
- PubMed (publishedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Keywords
- bicyclic peptides, phage display, affinity selection, protein-peptide interactions, constrained peptides, ligand characterization
- MeSH terms
- Bacteriophages, Ligands, Peptides, Cyclic, Peptide Library, Cell Surface Display Techniques
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