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A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits

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Published on: February 16, 2014

Chemokine-Binding All-D-CLIPS Peptides Identified Using Mirror-Image Phage Display.

Stepan S Denisov^1,2, Emilia L Bialek^2,3, Fabio Beretta³

¹Institute of Biological Chemistry, University of Vienna, Währinger Str. 38, 1090 Vienna, Austria.

ACS Chemical Biology

|October 29, 2025

Summary

This summary is machine-generated.

Researchers developed novel all-D-peptides that bind to the chemokine CXCL8, disrupting its function. These peptides show promise as therapeutic agents for inflammatory diseases by neutralizing specific chemokines.

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Area of Science:

Immunology
Biochemistry
Drug Discovery

Background:

Chemokines, such as C-X-C motif chemokine ligand 8 (CXCL8), are crucial for leukocyte migration during inflammation.
Neutralizing chemokines is a potential therapeutic strategy for inflammatory conditions.
Proteolytically stable peptides offer a promising avenue for developing chemokine-binding agents.

Purpose of the Study:

To develop novel, stable chemokine-binding peptides using mirror-image phage display.
To investigate the binding affinity and selectivity of all-D-peptides against CXCL8.
To assess the functional impact of these peptides on CXCL8 activity.

Main Methods:

Mirror-image phage display selection was employed to identify cyclic all-D-peptides targeting CXCL8.
Binding affinity and selectivity of selected peptides were characterized.
The effect of peptide binding on CXCL8 dimerization and glycosaminoglycan (GAG) binding was evaluated.

Main Results:

Structurally diverse all-D-peptides with submicromolar affinity for CXCL8 were successfully selected.
Selected peptides demonstrated varying selectivity towards related chemokines.
Peptide binding led to the dissociation of native CXCL8 dimers and disrupted CXCL8-GAG interactions.

Conclusions:

Mirror-image phage display is effective for selecting cyclic all-D-peptides against chemokines.
Developed all-D-peptides can neutralize CXCL8 by disrupting its structure and interactions.
These findings support the potential of all-D-peptides as therapeutic agents for chemokine-mediated inflammatory diseases.