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      Small Molecule Fluorescent Ligands for the Atypical Chemokine Receptor 3 (ACKR3)

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          Abstract

          The atypical chemokine receptor 3 (ACKR3) is a receptor that induces cancer progression and metastasis in multiple cell types. Therefore, new chemical tools are required to study the role of ACKR3 in cancer and other diseases. In this study, fluorescent probes, based on a series of small molecule ACKR3 agonists, were synthesized. Three fluorescent probes, which showed specific binding to ACKR3 through a luminescence-based NanoBRET binding assay (p K d ranging from 6.8 to 7.8) are disclosed. Due to their high affinity at the ACKR3, we have shown their application in both competition binding experiments and confocal microscopy studies showing the cellular distribution of this receptor.

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          CXCR7 Functions as a Scavenger for CXCL12 and CXCL11

          Ulrike Naumann, Elisabetta Cameroni, Monika Pruenster … (2010)
          Background CXCR7 (RDC1), the recently discovered second receptor for CXCL12, is phylogenetically closely related to chemokine receptors, but fails to couple to G-proteins and to induce typical chemokine receptor mediated cellular responses. The function of CXCR7 is controversial. Some studies suggest a signaling activity in mammalian cells and zebrafish embryos, while others indicate a decoy activity in fish. Here we investigated the two propositions in human tissues. Methodology/Principal Findings We provide evidence and mechanistic insight that CXCR7 acts as specific scavenger for CXCL12 and CXCL11 mediating effective ligand internalization and targeting of the chemokine cargo for degradation. Consistently, CXCR7 continuously cycles between the plasma membrane and intracellular compartments in the absence and presence of ligand, both in mammalian cells and in zebrafish. In accordance with the proposed activity as a scavenger receptor CXCR7-dependent chemokine degradation does not become saturated with increasing ligand concentrations. Active CXCL12 sequestration by CXCR7 is demonstrated in adult mouse heart valves and human umbilical vein endothelium. Conclusions/Significance The finding that CXCR7 specifically scavenges CXCL12 suggests a critical function of the receptor in modulating the activity of the ubiquitously expressed CXCR4 in development and tumor formation. Scavenger activity of CXCR7 might also be important for the fine tuning of the mobility of hematopoietic cells in the bone marrow and lymphoid organs.
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            FRED and HYBRID docking performance on standardized datasets.

            Mark McGann (2012)
            The docking performance of the FRED and HYBRID programs are evaluated on two standardized datasets from the Docking and Scoring Symposium of the ACS Spring 2011 national meeting. The evaluation includes cognate docking and virtual screening performance. FRED docks 70 % of the structures to within 2 Å in the cognate docking test. In the virtual screening test, FRED is found to have a mean AUC of 0.75. The HYBRID program uses a modified version of FRED's algorithm that uses both ligand- and structure-based information to dock molecules, which increases its mean AUC to 0.78. HYBRID can also implicitly account for protein flexibility by making use of multiple crystal structures. Using multiple crystal structures improves HYBRID's performance (mean AUC 0.80) with a negligible increase in docking time (~15 %).
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              AMD3100 is a CXCR7 ligand with allosteric agonist properties.

              B Limberg, Irina Kalatskaya, Yamina Berchiche … (2009)
              The bicyclam AMD3100 is known as a small synthetic inhibitor of the CXCL12-binding chemokine receptor CXCR4. Here, we show that AMD3100 also binds to the alternative CXCL12 receptor CXCR7. CXCL12 or AMD3100 alone activate beta-arrestin recruitment to CXCR7, which we identify as a previously unreported signaling pathway of CXCR7. In addition, AMD3100 increases CXCL12 binding to CXCR7 and CXCL12-induced conformational rearrangements in the receptor dimer as measured by bioluminescence resonance energy transfer. Moreover, small but reproducible increases in the potency of CXCL12-induced arrestin recruitment to CXCR7 by AMD3100 are observed. Taken together, our data suggest that AMD3100 is an allosteric agonist of CXCR7. The finding that AMD3100 not only binds CXCR4, but also to CXCR7, with opposite effects on the two receptors, calls for caution in the use of the compound as a tool to dissect CXCL12 effects on the respective receptors in vitro and in vivo.
              Article 0 comments Cited 90 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): ACS Med Chem Lett
                Journal ID (iso-abbrev): ACS Med Chem Lett
                Journal ID (publisher-id): ml
                Journal ID (coden): amclct
                Title: ACS Medicinal Chemistry Letters
                Publisher: American Chemical Society
                ISSN (Electronic): 1948-5875
                Publication date (Electronic): 08 December 2023
                Publication date Collection: 11 January 2024
                Publication date PMC-release: 08 December 2023
                Volume: 15
                Issue: 1
                Pages: 143-148
                Affiliations
                [† ]Biodiscovery Institute, School of Pharmacy, University of Nottingham , Nottingham NG7 2RD, United Kingdom
                [‡ ]Centre of Membrane Proteins and Receptors, University of Birmingham and University of Nottingham , The Midlands NG7 2UH, United Kingdom
                [§ ]Division of Physiology, Pharmacology & Neuroscience, Medical School, University of Nottingham , Nottingham NG7 2UH, U.K.
                [∥ ]Division of Medicinal Chemistry, Amsterdam Institute of Molecular and Life Sciences (AIMMS), Faculty of Science, Vrije Universiteit Amsterdam , De Boelelaan 1108, Amsterdam 1081 HZ, The Netherlands
                Author notes
                Author information
                https://orcid.org/0000-0002-7942-5006
                https://orcid.org/0000-0001-6331-5606
                https://orcid.org/0000-0003-1354-2848
                https://orcid.org/0000-0003-0030-9908
                https://orcid.org/0000-0002-4424-239X
                https://orcid.org/0000-0003-3046-137X
                Article
                DOI: 10.1021/acsmedchemlett.3c00469
                PMC ID: 10788940
                PubMed ID: 38229752
                SO-VID: 2b7fe1df-5fb8-403c-9b72-1460f4bbb0bc
                Copyright © © 2023 The Authors. Published by American Chemical Society
                License:

                Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained ( https://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 19 October 2023
                Date accepted : 29 November 2023
                Date revision received : 24 November 2023
                Funding
                Funded by: H2020 Marie Sklodowska-Curie Actions, doi 10.13039/100010665;
                Award ID: 641833
                Funded by: University of Nottingham, doi 10.13039/501100000837;
                Award ID: NA
                Funded by: Medical Research Council, doi 10.13039/501100000265;
                Award ID: MR/W016176/1
                Funded by: Medical Research Council, doi 10.13039/501100000265;
                Award ID: MR/N020081/1
                Funded by: H2020 Marie Sklodowska-Curie Actions, doi 10.13039/100010665;
                Award ID: 860229
                Categories
                Subject: Letter
                Custom metadata
                document-id-old-9 ml3c00469
                document-id-new-14 ml3c00469
                ccc-price

                ScienceOpen disciplines: Pharmaceutical chemistry
                Keywords: chemokine receptor,ackr3,cxcr7,fluorescent probes,bodipy,nanobret
                Data availability:
                ScienceOpen disciplines: Pharmaceutical chemistry
                Keywords: chemokine receptor, ackr3, cxcr7, fluorescent probes, bodipy, nanobret

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