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dc.contributor.authorMurphy, Paul V.
dc.contributor.authorRomero, Antonio
dc.contributor.authorXiao, Qi
dc.contributor.authorLudwig, Anna-Kristin
dc.contributor.authorJogula, Srinivas
dc.contributor.authorShilova, Nadezhda V.
dc.contributor.authorSingh, Tanuja
dc.contributor.authorGabba, Adele
dc.contributor.authorJaved, Bilal
dc.contributor.authorZhang, Dapeng
dc.contributor.authorMedrano, Francisco J.
dc.contributor.authorKaltner, Herbert
dc.contributor.authorKopitz, Jürgen
dc.contributor.authorBovin, Nicolai V.
dc.contributor.authorWu, Albert M.
dc.contributor.authorKlein, Michael L.
dc.contributor.authorPercec, Virgil
dc.contributor.authorGabius, Hans-Joachim
dc.identifier.citationMurphy, Paul V., Romero, Antonio, Xiao, Qi, Ludwig, Anna-Kristin, Jogula, Srinivas, Shilova, Nadezhda V., Singh, Tanuja, Gabba, Adele, Javed, Bilal, Zhang, Dapeng, Medrano, Francisco J., Kaltner, Herbert, Kopitz, Jürgen, Bovin, Nicolai V., Wu, Albert M., Klein, Michael L., Percec, Virgil, Gabius, Hans-Joachim. (2021). Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes. iScience, 24(1), 101919. doi:
dc.description.abstractThe small 3-O-sulfated galactose head group of sulfatides, an abundant glycosphingolipid class, poses the (sphinx-like) riddle on involvement of glycan bridging by tissue lectins (sugar code). First, synthesis of head group derivatives for functionalization of amphiphilic dendrimers is performed. Aggregation of resulting (biomimetic) vesicles, alone or in combination with lactose, demonstrates bridging by a tissue lectin (galectin-4). Physiologically, this can stabilize glycolipid-rich microdomains (rafts) and associate sulfatide-rich regions with specific glycoproteins. Further testing documents importance of heterobivalency and linker length. Structurally, sulfatide recognition by galectin-8 is shown to involve sphingosine's OH group as substitute for the 3′-hydroxyl of glucose of lactose. These discoveries underscore functionality of this small determinant on biomembranes intracellularly and on the cell surface. Moreover, they provide a role model to examine counterreceptor capacity of more complex glycans of glycosphingolipids and to start their bottom-up glycotope surface programming.en_IE
dc.description.sponsorshipThis work is supported by NSF Grants DMR1066116 , DMR-1720530 , and DMR-1807127 (to V.P.), the P. Roy Vagelos Chair at the University of Pennsylvania (V.P.), the Sheikh Saqr Research Foundation (to M.L.K.), the Science Foundation Ireland (SFI) and the European Regional Development Fund (Grant Number 13/RC/2073 to CÚRAM, 16/IA/4419 to P.V.M.), the European Union's Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No 713690 (Medtrain, to CÚRAM & S.J.), the Irish Research Council (PhD scholarship to A.G.), the Grant BFU2016-77835-R of the Spanish Ministry of Economy and Competitiveness (A.R.), as well as the COST Action CA18103 (InnoGly). We gratefully acknowledge inspiring discussions with Drs. B. Friday, A. Leddoz, and A.W.L. Nose, as well as the valuable recommendations by the reviewers.en_IE
dc.publisherCell Pressen_IE
dc.subjectSulfatide-Tissue Lectinen_IE
dc.subjectFunctionalized Glycodendrimersomesen_IE
dc.titleProbing sulfatide-tissue lectin recognition with functionalized glycodendrimersomesen_IE
dc.contributor.funderNational Science Foundationen_IE
dc.contributor.funderScience Foundation Irelanden_IE
dc.contributor.funderEuropean Regional Development Funden_IE
dc.contributor.funderHorizon 2020en_IE
dc.contributor.funderIrish Research Councilen_IE
dc.local.contactPaul Murphy, School Of Chemistry, Room 108, Arts/Science Building, Nui Galway. 2465 Email:
dcterms.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Centres/13/RC/2073/IE/C�RAM - Centre for Research in Medical Devices/en_IE
dcterms.projectinfo:eu-repo/grantAgreement/EC/H2020::MSCA-COFUND-FP/713690/EU/Career Development and Mobility Fellowships in Medical Device Research and Development: A CÚRAM Industry-Academia Training Initiative./MedTrainen_IE

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