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. 2017 Nov 13;56(46):14677-14681.
doi: 10.1002/anie.201708237. Epub 2017 Oct 10.

Reaction of a Programmable Glycan Presentation of Glycodendrimersomes and Cells With Engineered Human Lectins To Show the Sugar Functionality of the Cell Surface

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Reaction of a Programmable Glycan Presentation of Glycodendrimersomes and Cells With Engineered Human Lectins To Show the Sugar Functionality of the Cell Surface

Jürgen Kopitz et al. Angew Chem Int Ed Engl. .

Abstract

Chemical and biological tools are harnessed to investigate the impact of spatial factors for functional pairing of human lectins with counterreceptors. The homodimeric adhesion/growth-regulatory galectin-1 and a set of covalently linked homo-oligomers from di- to tetramers serve as proof-of-principle test cases. Glycodendrimersomes provide a versatile and sensitive diagnostic platform to reveal thresholds for ligand density and protein concentration in aggregation assays (trans-activity), irrespective of linker length between lectin domains. Monitoring the affinity of cell binding and ensuing tumor growth inhibition reveal the linker length to be a bidirectional switch for cis-activity. The discovery that two aspects of lectin functionality (trans- versus cis-activity) respond non-uniformly to a structural change underscores the power of combining synthetic and biological tools to advance understanding of the sugar functionality of the cell surface.

Keywords: agglutination; gangliosides; glycosylation; self-assembly; tumors.

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