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DTSTART;TZID=Europe/Paris:20260331T140000
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DTSTAMP:20260507T155823
CREATED:20260227T152048Z
LAST-MODIFIED:20260227T152234Z
UID:10000088-1774965600-1774969200@sfp-alpes.fr
SUMMARY:Simon PONTON (chargé de recherche CNRS - SIMaP)
DESCRIPTION:Development of the combinatorial approach for the CVD thin film deposition process : Multiphysics coupling and machine learning\nRésumé : \nThe combinatorial approach applied to chemical vapor deposition processes integrating high-throughput experiments\, computational simulations\, and machine learning seems to emerge as a transformative paradigm to accelerate the discovery of novel materials. Through systematic gradient explorations\, large-scale datasets can be generated to deepen our understanding of process-structure-property relationships. Machine learning models\, trained on experimental and simulated data enable rapid prediction and identification of high-potential solutions\, thereby guiding future experiments and simulations. The synergy not only reduces the time or cost associated with material discovery but also unlocks access to previously unexplored regions of the materials space. \nShort Bio/CVMy academic journey began in Grenoble\, where I studied chemistry before developing a keen interest in materials sciences\, particularly nanostructures and their processing. Driven by a desire to unravel the underlying mechanisms\, I started my PhD in Toulouse\, between the CIRIMAT and LGC. There\, I expanded my expertise in chemical engineering and Multiphysics simulation. After nearly two years of postdoctoral research\, I sought to broaden my research perspective and joined Polytechnique Montréal in the chemical engineering section for two postdoctoral positions that led to an associate professor role. However\, my longing for French cheese proved irresistible\, I successfully secured a position at CNRS and joined SIMaP in February 2026. \nContact : deborah.verger@grenoble-inp.fr
URL:https://sfp-alpes.fr/event/simon-ponton-charge-de-recherche-cnrs-simap/
LOCATION:LMGP – salle des séminaires\, Grenoble INP -Phelma 3 parvis Louis Néel\, Grenoble\, 38054\, France
CATEGORIES:Séminaire
ORGANIZER;CN="LMGP":MAILTO:deborah.verger@grenoble-inp.fr
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DTSTART;TZID=Europe/Paris:20260331T140000
DTEND;TZID=Europe/Paris:20260331T160000
DTSTAMP:20260507T155823
CREATED:20260227T101524Z
LAST-MODIFIED:20260227T151214Z
UID:10000082-1774965600-1774972800@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Espérance AHO (IBS/Groupe Structure et Activité des Glycosaminoglycanes)
DESCRIPTION:Structural and Functional effect of CXCL12/Heparan Sulfate Interactions at the Cell Surface\nRésumé : \nThe glycocalyx is a protective layer covering the surface of cells\, particularly endothelial cells\, and represents a major regulator of cell-environment interactions. It functions as a mechanical barrier\, a mechanosensor\, and a signalling platform that controls vascular permeability. In inflammatory and tumor contexts\, alterations in glycocalyx structure and density promote increased cell adhesion\, extravasation\, and metastatic dissemination. Structurally\, the glycocalyx is composed of glycolipids\, glycoproteins and proteoglycans bearing glycosaminoglycan (GAG) chains\, including heparan sulfate (HS). These linear polysaccharides\, organized into sulfated and non-sulfated domains\, interact with numerous proteins\, including growth factors and chemokines\, thereby modulating their bioavailability and biological activity. Notably\, chemokine-HS interactions are essential for the formation of chemotactic gradients involved in leukocyte recruitment\, inflammatory extravasation\, and tumor progression. The chemokine CXCL12 (stromal cell-derived factor-1\, SDF-1)\, a member of the CXC chemokine family\, exists as six distinct isoforms generated by alternative splicing of the CXCL12 gene. These isoforms share a common N-terminal sequence but differ in their C-terminal extensions\, which influence their interactions with HS. Among them\, CXCL12γ isoform\, characterized by its exceptionally high affinity for HS\, represent a particularly relevant candidate. \nThis work builds upon previous findings from our group showing\, using biophysical approaches (QCM-D\, FRAP)\, that CXCL12 is able to induce cross-linking of HS chains on biomimetic surfaces\, resulting in HS rigidification\, decreased layer thickness\, and reduced HS lateral mobility. These observations suggest that chemokine-HS interactions can modify the physical properties of HS beyond a simple ligand-presentation role. The central hypothesis of this project is that binding of the CXCL12γ to HS induces remodelling of the endothelial glycocalyx at the cell surface thereby changing cellular mechanical properties and promoting immune cell adhesion. Here\, we investigate the impact of CXCL12γ on HS organization across molecular\, nanoscale\, and cellular levels by combining biomimetic surfaces\, biophysical approaches\, super-resolution microscopy\, and cell-based assays. \nWe show that CXCL12γ reorganizes HS chains at the endothelial cell surface and that all HS-binding sites are required for efficient HS rigidification and network reorganization. CXCL12γ-driven remodeling of the glycocalyx reduces HS thickness and alters its nanoscale topology\, thereby promoting paracellular permeability and formation of adhesive platforms that facilitate leukocyte capture\, and firm adhesion. \nContact : ibs.seminaires@ibs
URL:https://sfp-alpes.fr/event/esperance-aho-ibs-groupe-structure-et-activite-des-glycosaminoglycanes/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
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