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

## TL;DR

Researchers developed stable peptides that bind to a specific chemokine, CXCL8, using a mirror-image phage display method, which could help treat inflammation-related diseases.

## Contribution

The study introduces the use of mirror-image phage display to identify proteolytically stable all-D-peptides with submicromolar affinity for CXCL8.

## Key findings

- All-D-peptides with submicromolar affinity to CXCL8 were identified using mirror-image phage display.
- These peptides disrupted CXCL8 dimerization and GAG binding without affecting cell migration.
- The peptides showed structural diversity and selectivity for CXCL8 over related chemokines.

## Abstract

Chemokines are secreted blood proteins that steer leukocyte
migration
in the inflammatory response. Neutralization of chemokines is believed
to be a beneficial therapeutic strategy for the treatment of inflammation-associated
diseases. Proteolytically stable chemokine-binding peptides could
be suitable candidates for the development of chemokine-neutralizing
agents. Here, we report the mirror-image phage display selection of
cyclic all-D-peptides against the C–X–C motif chemokine
ligand 8 (CXCL8). Selection yielded structurally diverse all-D-peptides
with submicromolar affinity to the target CXCL8 chemokine and different
selectivity to related chemokines. Binding of these all-D-peptides
caused dissociation of the native CXCL8 dimer and disruption of its
binding to GAGs, without an effect on in vitro cell migration. This
work demonstrates the example of mirror-image phage display selection
of cyclized all-D-peptides and its utility for the development of
chemokine-binding agents.