Evidence map›Paper›PMID 41157908›Full record

ArticleACS chemical biology2025

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

Stepan S Denisov, Emilia L Bialek, Fabio Beretta, Gintare Smagurauskaite, Hans Ippel, Eline Fijlstra, Sangram S Kale, Peter Timmerman, Tilman M Hackeng, Paul Proost and 2 more

Abstract read
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In one paragraph

Article in ACS chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Phage Display as a Promising Platform for Peptide Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2026
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Stepan S DenisovInstitute of Biological Chemistry, University of Vienna, Währinger Str. 38, 1090 Vienna, Austria.ORCID 0000-0001-5460-940X
Emilia L BialekDepartment of Biochemistry, Maastricht University, Cardiovascular Research Institute Maastricht (CARIM), Universiteitssingel 50, 6229 ER Maastricht, The Netherlands.
Fabio BerettaRega Institute, KU Leuven, Herestraat 49, 3000 Leuven, Belgium.ORCID 0000-0001-9369-2525
Gintare SmagurauskaiteRDM Cardiovascular Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, U.K.
Hans IppelDepartment of Biochemistry, Maastricht University, Cardiovascular Research Institute Maastricht (CARIM), Universiteitssingel 50, 6229 ER Maastricht, The Netherlands.
Eline FijlstraBiosynth B.V., Zuidersluisweg 2, 8243 RC Lelystad, The Netherlands.
Sangram S KaleBiosynth B.V., Zuidersluisweg 2, 8243 RC Lelystad, The Netherlands.
Peter TimmermanBiosynth B.V., Zuidersluisweg 2, 8243 RC Lelystad, The Netherlands.
Tilman M HackengDepartment of Biochemistry, Maastricht University, Cardiovascular Research Institute Maastricht (CARIM), Universiteitssingel 50, 6229 ER Maastricht, The Netherlands.
Paul ProostRega Institute, KU Leuven, Herestraat 49, 3000 Leuven, Belgium.
Michael GoldflamBiosynth B.V., Zuidersluisweg 2, 8243 RC Lelystad, The Netherlands.
Ingrid DijkgraafDepartment of Biochemistry, Maastricht University, Cardiovascular Research Institute Maastricht (CARIM), Universiteitssingel 50, 6229 ER Maastricht, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

ChemokinesInterleukin-8Peptide LibraryPeptidesPeptides, CyclicAmino Acid SequenceHumansProtein BindingChemokinesCXCL8 protein, humanInterleukin-8Peptide LibraryPeptidesPeptides, Cyclic

Identifiers

PMID41157908
PMCPMC12645432

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.