---
title: "De novo macrocyclic peptides yield potent CXCR4 antagonists for class A GPCRs"
id: "biorxiv-22-de-novo-macrocyclic-peptide-discovery-produces-potent-class-a-gpcr-ligands-with"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-22-de-novo-macrocyclic-peptide-discovery-produces-potent-class-a-gpcr-ligands-with"
content_type: "clinical_feed_article"
specialty: "Pharmacology"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.10.21.760615v1?rss=1"
published_at: "2026-10-22T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# De novo macrocyclic peptides yield potent CXCR4 antagonists for class A GPCRs
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-22-de-novo-macrocyclic-peptide-discovery-produces-potent-class-a-gpcr-ligands-with
- **Specialty:** [Pharmacology](https://medichelpline.com/clinical-feed/pharmacology.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.10.21.760615v1?rss=1)
- **Published At:** 2026-10-22T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- Investigators applied the random nonstandard peptides integrated discovery platform (**RaPID**) to generate **de novo** macrocyclic peptides directed against the class A GPCR **CXCR4**. - The study targeted **CXCR4** because of its roles in cell migration, immune surveillance, inflammation and as an HIV entry co-receptor. - The discovery campaign produced novel peptides that bound within the receptor’s orthosteric pocket, according to the authors. - Lead peptides demonstrated **nanomolar affinity** for **CXCR4** in the assays reported. - The study team observed antagonism of receptor signaling by the most active compounds. - Functional readouts included suppression of chemokine-driven cell migration and blockade of **CXCR4**-mediated HIV entry. - Data indicated selectivity for **CXCR4** among the agents described. - The authors emphasized that class A GPCRs, despite a structurally limited solvent-exposed surface, can be targeted by macrocyclic peptides. - The article is a preprint and has not been peer reviewed; the source did not report certain experimental details such as exact library sizes, selection stringency, dosing or sample sizes. - Remaining questions include generalizability to other class A GPCRs, in vivo activity, pharmacokinetics, and safety; the preprint did not provide these data.
## Clinical Analysis & Structured Key Points
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Fernando Salgado-Polo 1 Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Fernando%2BSalgado-Polo%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Salgado-Polo%20F&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AFernando%2BSalgado-Polo%2B) * [ORCID record for Fernando Salgado-Polo](http://orcid.org/0000-0001-8362-5281 "Open in new tab") Marin Matic 2 Department of Drug Design and Pharmacology, Center for Pharmaceutical Data Science Education, University of Copenhagen, Copenhagen, Denmark; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Marin%2BMatic%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Matic%20M&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AMarin%2BMatic%2B) * [ORCID record for Marin Matic](http://orcid.org/0000-0003-1449-8797 "Open in new tab") Philip Ben Rainsford 1 Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Philip%2BBen%2BRainsford%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Rainsford%20PB&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3APhilip%2BBen%2BRainsford%2B) * [ORCID record for Philip Ben Rainsford](http://orcid.org/0000-0002-0434-4586 "Open in new tab") Felix Faas 1 Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Felix%2BFaas%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Faas%20F&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AFelix%2BFaas%2B) * [ORCID record for Felix Faas](http://orcid.org/0000-0002-2596-045X "Open in new tab") Max Meyrath 3 Immuno-Pharmacology and Interactomics, Department of Infection and Immunity, Luxembourg Institute of Health, Esch-sur-Alzette 4354, Luxembourg; 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* [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Martin%2BGustavsson%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Gustavsson%20M&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AMartin%2BGustavsson%2B) * [ORCID record for Martin Gustavsson](http://orcid.org/0000-0002-3015-2043 "Open in new tab") * For correspondence: martin@sund.ku.dk * [Abstract](https://www.biorxiv.org/content/10.64898/2026.10.21.760615v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5891840/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.10.21.760615v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5891840/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.10.21.760615v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5891840/1) * [Supplementary material](https://www.biorxiv.org/content/10.64898/2026.10.21.760615v1.supplementary-material)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_data/node:5891840/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.10.21.760615v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5891840/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract G protein-coupled receptors (GPCRs) represent one of the largest protein families of therapeutic importance, as over one third of all currently approved drugs target GPCRs. A growing proportion of GPCR drugs are peptides. However, class A GPCRs (over 80% of clinically studied targets) are underexploited as peptide targets, presumably since their only structured domain is the core, seven-helix, integral membrane fold presenting a limited solvent-exposed surface area. Screening libraries of _de novo_ macrocyclic peptides have allowed for the targeting of otherwise intractable proteins, but their potential to generate selective ligands for class A GPCRs has not been demonstrated. Here, we used random nonstandard peptides integrated discovery (RaPID) to identify de novo macrocyclic peptide ligands targeting the chemokine receptor CXCR4. CXCR4 regulates cell migration, immune surveillance, and inflammation, making it an important therapeutic target for multiple diseases. We discovered novel, potent CXCR4-selective antagonists binding within the orthosteric pocket with nanomolar affinity. The most active peptides effectively inhibited receptor signaling, suppressed chemokine-driven cell migration, and blocked CXCR4-driven HIV entry. Our results show that even the structurally minimal class A GPCRs are viable targets for de novo cyclic peptide discovery, highlighting the potential for uncovering ligands towards other members of the GPCR superfamily. ### Competing Interest Statement The authors declare the following financial interests/personal relationships which may
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