2024-03-28T08:25:47Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1598482020-11-13T13:43:20Zcom_10261_86com_10261_1col_10261_339
00925njm 22002777a 4500
dc
Kopitz, Jürgen
author
Romero, Antonio
author
Percec, V.
author
2017-11-13
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.
Angew Chem Int Ed Engl. 56(46):14677-14681 (2017)
1433-7851
http://hdl.handle.net/10261/159848
10.1002/anie.201708237
1521-3773
http://dx.doi.org/10.13039/100000001
Agglutination
Gangliosides
Glycosylation
Self-assembly
Tumors
Reaction of a programmable glycan presentation of glycodendrimersomes and cells with engineered human lectins to show the sugar functionality of the cell surface