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000885454 1001_ $$0P:(DE-HGF)0$$aHoffmann, Marius$$b0$$eCorresponding author
000885454 245__ $$aSynthesis of the Thomsen-Friedenreich-antigen (TF-antigen) and binding of Galectin-3 to TF-antigen presenting neo-glycoproteins
000885454 260__ $$aDordrecht [u.a.]$$bSpringer Science + Business Media B.V$$c2020
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000885454 520__ $$aThe Thomsen-Friedenreich-antigen, Gal(β1–3)GalNAc(α1-O-Ser/Thr (TF-antigen), is presented on the surface of most human cancer cell types. Its interaction with galectin 1 and galectin 3 leads to tumor cell aggregation and promotes cancer metastasis and T-cell apoptosis in epithelial tissue. To further explore multivalent binding between the TF-antigen and galectin-3, the TF-antigen was enzymatically synthesized in high yields with GalNAc(α1-EG3-azide as the acceptor substrate by use of the glycosynthase BgaC/Glu233Gly. Subsequently, it was coupled to alkynyl-functionalized bovine serum albumin via a copper(I)-catalyzed alkyne-azide cycloaddition. This procedure yielded neo-glycoproteins with tunable glycan multivalency for binding studies. Glycan densities between 2 and 53 glycan residues per protein molecule were obtained by regulated alkynyl-modification of the lysine residues of BSA. The number of coupled glycans was quantified by sodium dodecyl sulfate polyacrylamide gel electrophoresis and a trinitrobenzene sulfonic acid assay. The binding efficiency of the neo-glycoproteins with human galectin-3 and the effect of multivalency was investigated and assessed using an enzyme-linked lectin assay. Immobilized neo-glycoproteins of all modification densities showed binding of Gal-3 with increasing glycan density. However, multivalent glycan presentation did not result in a higher binding affinity. In contrast, inhibition of Gal-3 binding to asialofetuin was effective. The relative inhibitory potency was increased by a factor of 142 for neo-glycoproteins displaying 10 glycans/protein in contrast to highly decorated inhibitors with only 2-fold increase. In summary, the functionality of BSA-based neo-glycoproteins presenting the TF-antigen as multivalent inhibitors for Gal-3 was demonstrated.
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000885454 7001_ $$0P:(DE-Juel1)159276$$aHayes, Marc R.$$b1
000885454 7001_ $$0P:(DE-Juel1)128906$$aPietruszka, Jörg$$b2
000885454 7001_ $$0P:(DE-HGF)0$$aElling, Lothar$$b3$$eCorresponding author
000885454 773__ $$0PERI:(DE-600)1483682-8$$a10.1007/s10719-020-09926-y$$gVol. 37, no. 4, p. 457 - 470$$n4$$p457 - 470$$tGlycoconjugate journal$$v37$$x1573-4986$$y2020
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