18 research outputs found
Chemical Characterization of α-Oxohydrazone Ligation on Colloids: toward Grafting Molecular Addresses onto Biological Vectors
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"Synthesis of Chemical Tools Toward a Structure /Properties Relationships Study onto Targeting Colloids"
Anchorage of synthetic peptides onto liposomes via hydrazone and alpha-oxo hydrazone bonds. Preliminary functional investigations
Novel powerful water-soluble lipid immunoadjuvants inducing mouse dendritic cell maturation and B cell proliferation using TLR2 pathway.
Item does not contain fulltextFour novel water-soluble lipid immunoadjuvants were designed, synthesized and characterized by MS and NMR. They all induce mouse dendritic cell maturation and B cell proliferation. We demonstrate that in spite of the chemical modification, the four compounds remain TLR2 agonists
Grafting of synthetic mannose receptor-ligands onto onion vectors for human dendritic cells targetingElectronic supplementary information (ESI) available: full experimental details. See http://www.rsc.org/suppdata/cc/b2/b206980f/
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Proteomic analysis of adaptor protein 1A coats selectively assembled on liposomes
Coat components localize to specific membrane domains, where they sort selected transmembrane proteins. To study how clathrin coats are stabilized on such domains and to identify the protein networks involved, we combined proteomic screens and in vitro liposome-based assays that recapitulate the fidelity of protein sorting in vivo. Our study identifying ≈40 proteins on AP-1A-coated liposomes revealed that AP-1A coat assembly triggers the concomitant recruitment of Rac1, its effectors, and the Wave/Scar complex as well as that of Rab11 and Rab14. The coordinated recruitment of these different machineries requires a mosaic of membrane components comprising the GTPase ADP-ribosylation factor 1, sorting signals in selected transmembrane proteins, and phosphatidylinositol 4-phosphate. These results demonstrate that the combinatorial use of low-affinity binding sites present on the same membrane domain accounts not only for a selective coat assembly but also for the coordinated assembly of selected machineries required for actin polymerization and subsequent membrane fusion