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| Home > Publications database > Synthesis of the Thomsen-Friedenreich-antigen (TF-antigen) and binding of Galectin-3 to TF-antigen presenting neo-glycoproteins > print |
| Home > Publications database > Synthesis of the Thomsen-Friedenreich-antigen (TF-antigen) and binding of Galectin-3 to TF-antigen presenting neo-glycoproteins > print |
| 001 | 885454 | ||
| 005 | 20210130010412.0 | ||
| 024 | 7 | _ | |a 10.1007/s10719-020-09926-y |2 doi |
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| 024 | 7 | _ | |a 1573-4986 |2 ISSN |
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| 100 | 1 | _ | |a Hoffmann, Marius |0 P:(DE-HGF)0 |b 0 |e Corresponding author |
| 245 | _ | _ | |a Synthesis of the Thomsen-Friedenreich-antigen (TF-antigen) and binding of Galectin-3 to TF-antigen presenting neo-glycoproteins |
| 260 | _ | _ | |a Dordrecht [u.a.] |c 2020 |b Springer Science + Business Media B.V |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a The 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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| 700 | 1 | _ | |a Hayes, Marc R. |0 P:(DE-Juel1)159276 |b 1 |
| 700 | 1 | _ | |a Pietruszka, Jörg |0 P:(DE-Juel1)128906 |b 2 |
| 700 | 1 | _ | |a Elling, Lothar |0 P:(DE-HGF)0 |b 3 |e Corresponding author |
| 773 | _ | _ | |a 10.1007/s10719-020-09926-y |g Vol. 37, no. 4, p. 457 - 470 |0 PERI:(DE-600)1483682-8 |n 4 |p 457 - 470 |t Glycoconjugate journal |v 37 |y 2020 |x 1573-4986 |
| 856 | 4 | _ | |y OpenAccess |u https://juser.fz-juelich.de/record/885454/files/Hoffmann2020_Article_SynthesisOfTheThomsen-Friedenr.pdf |
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