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DTSTART;TZID=Europe/Paris:20260306T110000
DTEND;TZID=Europe/Paris:20260306T120000
DTSTAMP:20260617T191646
CREATED:20260227T090909Z
LAST-MODIFIED:20260227T091022Z
UID:10000076-1772794800-1772798400@sfp-alpes.fr
SUMMARY:Kilian FRABOULET (Max Planck Institute Stuttgart)
DESCRIPTION:Competing orders in many-electron systems: a renormalization group perspective\nRésumé :  \nThe renormalization group is an established approach to study quantum many-body systems\, and this applies especially to one of its modern implementations known as the functional renormalization group (fRG). In particular\, the fRG constitutes a flexible and unbiased tool for the study of competing orders. In this talk\, I will outline recent progress in this direction for correlated electron systems. To this end\, I will first discuss the competition between antiferromagnetism\, charge density waves and superconductivity in the 2D Hubbard model\, thus making a connection with high-temperature superconductors. The special role of bosonization methods will be emphasized along the way. I will also show how the fRG can be combined with dynamical mean-field theory to treat strongly interacting regimes\, with a focus on d-wave superconductivity. As a next step\, I will increase the complexity of the model by including non-local interactions and discuss unconventional superconductivity in an extended Hubbard model with a connection to moiré materials. Special consideration will also be given to the treatment of retarded interactions with electron-phonon couplings. Finally\, I will highlight recent fRG studies of quantum criticality in Dirac materials\, with a connection to graphene. \nContact : serge.florens@neel.cnrs.fr
URL:https://sfp-alpes.fr/event/kilian-fraboulet-max-planck-institute-stuttgart/
LOCATION:LPMMC – salle Roger Maynard (G421)\, CNRS - LPMMC 25 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
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DTSTART;TZID=Europe/Paris:20260306T140000
DTEND;TZID=Europe/Paris:20260306T150000
DTSTAMP:20260617T191646
CREATED:20260305T145615Z
LAST-MODIFIED:20260305T145620Z
UID:10000093-1772805600-1772809200@sfp-alpes.fr
SUMMARY:Carlo PIFFERI (Centre de Biophysique Moléculaire\, Orléans)
DESCRIPTION:Exploiting disulfide-rich peptides as protein epitope mimics : development of a generalizable conjugation approach for immunogen preparation\nRésumé : \nGeneration of specific antibodies against peptides by immunization requires their covalent conjugation to protein carriers to override their inherently weak immunogenicity. The vast majority of bioconjugation approaches to achieve peptide-protein constructs rely on thiol-maleimide chemistry1 and capitalize on a wide array of commercial maleimide-functionalized protein carriers. Disulfide-rich peptides2 (DRPs) possess a rigid\, constrained structure that makes them ideal for designing synthetic mimics of protein regions/domains. For bioconjugation purposes\, the introduction of a single spare thiol moiety into a linear peptide antigen is straightforward\, while DRPs’ disulfide bonds are prone to intramolecular thiophilic attack by the reactive thiolate. This unintended reactivity competes with the desired Michael addition to the maleimide moiety\, ultimately disrupting the native disulfide bridging framework. As a result\, DRP’s tertiary structure will be altered\, affording an immunogen that is a poor mimic of the native target. Although a few studies have explored the late-stage introduction of thiol-containing cross-linkers onto DRP antigens for their conjugation onto protein carriers\,3\,4 the stability of DRP’s disulfide pattern in the presence of an extra thiol has never been examined. To address this\, we systematically evaluated the influence of different spacers in “DRP-spacer-thiol” constructs\, under thiol-maleimide reaction conditions.5 Our results highlight how both linker length and flexibility are key to maintain DRP disulfides unaltered\, providing a general approach to achieve DRP bioconjugation by thiol-maleimide chemistry. We have applied our approach to a small DRP predicted to closely mimic a surface-accessible epitope of the full LINGO-1 protein\, and obtained a very specific antibody response upon immunization: the resulting polyclonal IgG was able to selectively bind the full-length protein in a cellular context\, with stringent selectivity across its four homologs. \nReferences : \n1. M. Góngora-Benítez\, J. Tulla-Puche & F. Albericio\, Chem. Rev. 2014\, 114\, 901–926.\n2. K. Renault\, J. W. Fredy\, P.-Y. Renard & C. Sabot\, Bioconjug. Chem. 2018\, 29\, 2497–2513.\n3. H. Katayama & M. Mita\, Bioorganic Med. Chem. 2016\, 24\, 3596–3602.\n4. H. Katayama\, R. Mizuno & M. Mita\, Biosci. Biotechnol. Biochem. 2019\, 83\, 1791–1799.\n5. L. Azzoug et al.\, ChemRxiv 2025\, DOI:10.26434/chemrxiv-2025-krjcm \n_ \nContact : david.goyard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/carlo-pifferi-centre-de-biophysique-moleculaire-orleans/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
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