Laboratoire Léon-Brillouin (LLB), UMR12 CEA, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France
Tél. : +33 1 69 08 67 20
Email : sophie.combet@cea.fr
Function
CNRS Director of Research at the LLB
Scientific activity
I focus on the impact of ligand binding on protein structure through two primary projects: (i) the TSPO membrane protein, an essential neuroimaging marker with a high affinity for pharmacological ligands, and (ii) phycobiliproteins, such as C-phycocyanin, to investigate how interactions with bioactive ligands under pressure treatment influence their stability, with applications in the food industry.
I combine low-resolution techniques (SAXS/SANS), modeling approaches (e.g. ab initio, hybrid, interactive simulations), and higher-resolution structural methods (crystallography, cryo-EM) in close collaboration with I2BC (Saclay), IBPC (Paris), and MLZ (Germany).
Publication list
Selected recent publications
Minic S, Velickovic L, Thureau A, Gligorijevic N, Brûlet A, Combet* S. Probing the structural stability of R-phycocyanin under pressure. Prot Sci 33:e5145, 2024. https://doi.org/10.1002/pro.5145
Saade C, Pozza A, Bonnete F, Finet S, Lutz-Bueno V, Tully MD, Varela PF, Lacapere JJ, Combet* S. Enhanced structure/function of mTSPO translocator in lipid :surfactant mixed micelles. Biochimie 224, 3, 2024. https://doi.org/10.1016/j.biochi.2024.04.008
Minic S, Annighöfer B, Milcic M, Maignen F, Brûlet A, Combet* S. The effects of biliverdin on pressure-induced unfolding of apomyoglobin : The specific role of Zn2+ ions. Int J Biol Macromol 245, 125549, 2023. https://doi.org/10.1016/j.ijbiomac.2023.125549
Combet* S, Bonneté F, Finet S, Pozza A, Saade C, Martel A, Koutsioubas A, Lacapère JJ. Effect of amphiphilic environment on the solution structure of mouse TSPO translocator protein. Biochimie 205, 61-72, 2023. https://doi.org/10.1016/j.biochi.2022.11.014
Minic S, Annighöfer B, Hélary A, Sago L, Cornu D, Brûlet A, Combet* S. Structure of proteins under pressure: covalent binding effects of biliverdin on beta-lactoglobulin, Biophysical J, 121, 1, 2022. https://doi.org/10.1016/j.bpj.2022.06.003
Minic S, Annighöfer B, Hélary A, Hamdane D, Hui Bon Hoa G, Loupiac C, Brûlet A, Combet* S. Effect of ligands on HP-induced unfolding and oligomerization of β-lactoglobulin. Biophysical J 119 : 2262-2274, 2020. https://doi.org/10.1016/j.bpj.2020.10.019
Combet S, Cousin F, Rezaei H, Noinville S. Membrane interaction of off-pathway prion oligomers and lipid-induced on-pathway intermediates during prion conversion: a clue for neurotoxicity. Biochim Biophys Acta Biomembr 1861: 514, 2019. DOI: 10.1016/j.bbamem.2018.12.001
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet* S, Hubert* JF. Human dystrophin structural changes upon binding to anionic membrane lipid. Biophys J 115: 1231, 2018. DOI: 10.1016/j.bpj.2018.07.039
Chevreuil M, Law-Hine D, Chen J, Bressanelli S, Combet S, Constantin D, Degrouard J, Möller J, Zeghal M, Tresset G. Nonequilibrium self-assembly dynamics of icosahedral viral capsids packaging genome or polyelectrolyte. Nature Comm 9: 3071, 2018. DOI: 10.1038/s41467-018-05426-8