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Título

Reaction of a programmable glycan presentation of glycodendrimersomes and cells with engineered human lectins to show the sugar functionality of the cell surface

AutorKopitz, Jürgen; Romero, Antonio ; Percec, V.
Palabras claveAgglutination
Gangliosides
Glycosylation
Self-assembly
Tumors
Fecha de publicación13-nov-2017
EditorJohn Wiley & Sons
CitaciónAngew Chem Int Ed Engl. 56(46):14677-14681 (2017)
ResumenChemical 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.
Descripción10 p.-6 fig.-22 p. inf. supl. Kopitz, Jürgen et al.
Versión del editorhttp://dx.doi.org/10.1002/anie.201708237
URIhttp://hdl.handle.net/10261/159848
DOI10.1002/anie.201708237
ISSN1433-7851
E-ISSN1521-3773
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