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Article

Enzymatic Synthesis of N-Acetyllactosamine (LacNAc) Type 1 Oligomers and Characterization as Multivalent Galectin Ligands

Laboratory for Biomaterials, Institute for Biotechnology and Helmholtz-Institute for Biomedical Engineering, RWTH Aachen University, Pauwelsstraße 20, 52074 Aachen, Germany
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Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2017, 22(8), 1320; https://doi.org/10.3390/molecules22081320
Received: 14 June 2017 / Revised: 7 August 2017 / Accepted: 8 August 2017 / Published: 10 August 2017
(This article belongs to the Special Issue Synthesis and Biological Applications of Glycoconjugates)
Repeats of the disaccharide unit N-acetyllactosamine (LacNAc) occur as type 1 (Galβ1, 3GlcNAc) and type 2 (Galβ1, 4GlcNAc) glycosylation motifs on glycoproteins and glycolipids. The LacNAc motif acts as binding ligand for lectins and is involved in many biological recognition events. To the best of our knowledge, we present, for the first time, the synthesis of LacNAc type 1 oligomers using recombinant β1,3-galactosyltransferase from Escherichia coli and β1,3-N-acetylglucosaminyltranferase from Helicobacter pylori. Tetrasaccharide glycans presenting LacNAc type 1 repeats or LacNAc type 1 at the reducing or non-reducing end, respectively, were conjugated to bovine serum albumin as a protein scaffold by squarate linker chemistry. The resulting multivalent LacNAc type 1 presenting neo-glycoproteins were further studied for specific binding of the tumor-associated human galectin 3 (Gal-3) and its truncated counterpart Gal-3∆ in an enzyme-linked lectin assay (ELLA). We observed a significantly increased affinity of Gal-3∆ towards the multivalent neo-glycoprotein presenting LacNAc type 1 repeating units. This is the first evidence for differences in glycan selectivity of Gal-3∆ and Gal-3 and may be further utilized for tracing Gal-3∆ during tumor progression and therapy. View Full-Text
Keywords: neo-glycoproteins; biocatalysis; LacNAc type 1; chemo-enzymatic synthesis; one-pot; sequential; glycosyltransferase; galectin-3; multivalency neo-glycoproteins; biocatalysis; LacNAc type 1; chemo-enzymatic synthesis; one-pot; sequential; glycosyltransferase; galectin-3; multivalency
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MDPI and ACS Style

Fischöder, T.; Laaf, D.; Dey, C.; Elling, L. Enzymatic Synthesis of N-Acetyllactosamine (LacNAc) Type 1 Oligomers and Characterization as Multivalent Galectin Ligands. Molecules 2017, 22, 1320. https://doi.org/10.3390/molecules22081320

AMA Style

Fischöder T, Laaf D, Dey C, Elling L. Enzymatic Synthesis of N-Acetyllactosamine (LacNAc) Type 1 Oligomers and Characterization as Multivalent Galectin Ligands. Molecules. 2017; 22(8):1320. https://doi.org/10.3390/molecules22081320

Chicago/Turabian Style

Fischöder, Thomas, Dominic Laaf, Carina Dey, and Lothar Elling. 2017. "Enzymatic Synthesis of N-Acetyllactosamine (LacNAc) Type 1 Oligomers and Characterization as Multivalent Galectin Ligands" Molecules 22, no. 8: 1320. https://doi.org/10.3390/molecules22081320

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