ARPEGE platform
Facility, Pharmacology – Screening – Interactom



The ARPEGE platform is dedicated to extensive analysis of the structural and functional features of protein complexes. It allows the characterization of all kinds of specific interactions either between ligand and target, protein partners, and signaling complexes. The ARPEGE platform is managed by a team of highly experienced receptor biology and luminescence-based technique specialists. Its service offer is made available to academic laboratories, biotech as well as pharma and other industrial companies.
The platform offers its services on a fee-for-service basis to public laboratories and companies. We offer either open-access services (after appropriate training, customers have access to the equipment to carry out their project), or project/service agreements (platform engineers carry out all the experiments in accordance with the customer).
The ARPEGE facility is certified IBiSA and ISO:9001v2015 (since 2014).
More information on www.arpege.cnrs.fr
ARPEGE is a BioCampus plateform.

Screening of a small series of molecules on mu-opioid receptor signaling.











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2006PhD in Biology & Health - University Montpellier I - France
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2002MSc Immunotechnology - University Aix Marseille II - France
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2001MSc Biochemistry - University Montpellier II - France
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2012Technical Manager of the ARPEGE facility "Pharmacology - Screening - Interactome" - Institute of Functional Genomics - Montpellier - France
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2011Development Manager at Ciloa - University Montpellier II - France
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2007-2011Postdoctoral fellow - Ecole Polytechnique Fédérale de Lausanne - Switzerland
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2003-2006PhD student (IGF - CisBio Bioassays) - University Montpellier I - France
- Development of luminescence techniques (fluorescence, BRET, TR-FRET, HTRF), programming of pipetting robots
- Pharmacological analyses: molecular interactions (ligand-target binding, signalling pathways)
- Quality system management: maintenance and development of the quality system
- Management of the platform: management of services, R&D projects
- Teaching, training: training of customers in software, oral presentations




IGF Publications
- Dumazer A, Gómez-Santacana X, Malhaire F, Jopling C, Maurel D, Lebon G, Llebaria A, Goudet C. Optical control of adenosine A2A receptor using istradefylline photosensitivity. ACS Chemical Neurosciences. 2024 doi.org/10.1021/acschemneuro.3c00721
- Cong X, Maurel D, Déméné H, Vasiliauskaité-Brooks I, Hagelberger J, PeyssonF, Saint-Paul J, Golebiowski J, Granier S, Sounier R. Molecular insights into the biased signaling mechanism of the μ-opioid receptor. Molecular Cell. 2021 doi: 10.1016/j.molcel.2021.07.033
- Healey RD, Saied EM, Cong X, Karsai G, Gabellier L, Saint Paul J, Del Nero E, Jeannot S, Drapeau M, Fontanel S, Maurel D, Basu S, Leyrat C, Golebiowski J, Bossis G, Bechara C, Hornemann T, Arenz C, Granier S. Discovery and mechanism of action of small molecule inhibitors of ceramidases. Angewandte Chemie. 2021 doi.org/10.1002/anie.202109967
- Zindel D , Mensat P , Vol C , Homayed Z , Charrier-Savournin F , Trinquet E , Banères JL, Pin JP , Pannequin J , Roux T , Dupuis E, Prézeau G protein-coupled receptors can control the Hippo/YAP pathway through Gq signaling. FASEB J. 2021 doi: 10.1096/fj.202002159R.
Publications external to IGF
- Kampen S, Rodríguez D, Jørgensen M, Kruszyk-Kujawa M, Huang X, Collins M, Boyle N, Maurel D, Rudling A, Lebon G, and Carlsson J. Structure-Based Discovery of Negative Allosteric Modulators of the 2 Metabotropic Glutamate Receptor 5. ACS Chem Biol. 2022 doi: 10.1021/acschembio.2c00234
- Liu J, Hengmin Tang, Xu C, Zhou S, Zhu X, Li Y, Prézeau L, Xu T, Pin JP, Rondard P, Ji W, Liu J. Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor. Nat Commun. 2022; 13: 6365. doi: 10.1038/s41467-022-34056-4
- Mills, N. Aissaoui, D. Maurel, J. Elezgaray, F. Morvan, J. J. Vasseur, E. Margeat, R. B. Quast, J. Lai Kee-Him, N. Saint, C. Benistant, A. Nord, F. Pedaci, G. Bellot. A modular spring-loaded actuator for mechanical activation of membrane proteins. Nature Com. 2022 doi: 10.1038/s41467-022-30745-2