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@ARTICLE{Hoffmann:885454,
      author       = {Hoffmann, Marius and Hayes, Marc R. and Pietruszka, Jörg
                      and Elling, Lothar},
      title        = {{S}ynthesis of the {T}homsen-{F}riedenreich-antigen
                      ({TF}-antigen) and binding of {G}alectin-3 to {TF}-antigen
                      presenting neo-glycoproteins},
      journal      = {Glycoconjugate journal},
      volume       = {37},
      number       = {4},
      issn         = {1573-4986},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {FZJ-2020-03837},
      pages        = {457 - 470},
      year         = {2020},
      abstract     = {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.},
      cin          = {IBOC / IBG-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBOC-20090406 / I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32367478},
      UT           = {WOS:000530293700002},
      doi          = {10.1007/s10719-020-09926-y},
      url          = {https://juser.fz-juelich.de/record/885454},
}