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We have investigated the consequences of introducing a bisecting GlcNAc moiety into biantennary N-glycans. Computational analysis of glycan conformation with pro-longed simulation periods in vacuo and in a solvent box revealed two main effects: backfolding of thea1–6 arm and stacking of the bisectingGlcNAc and the neighboring Man/ GlcNAc residues of both antennae.Chemoenzymatic syn-thesis produced the bisecting biantennary decasaccharide N-glycan and itsa2–3(6)-sialylated variants. | Eur. J. Biochem. 271 118-134 2004 FEBS 2003 doi 10.1046 j.1432-1033.2003.03910.x Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico in vitro and in vivo Sabine Andre1 Carlo Unverzagt2 Shuji Kojima3 Martin Frank4 Joachim Seifert2 t Christian Fink5 Klaus Kayser6 Claus-Wilhelm von der Lieth4 and Hans-Joachim Gabius1 1Institut fur Physiologische Chemie Tierarztliche Fakulteit Ludwig-Maximilians-Universitat MUnchen Germany 2Institut fur Organische Chemie und Biochemie Technische Universităt Munchen Garching Germany 3Faculty of Pharmaceutical Sciences Tokyo University of Science Japan 4Zentrale Spektroskopie Deutsches Krebsforschungszentrum Heidelberg Germany 5Radiologische Diagnostik und Therapie Deutsches Krebsforschungszentrum Heidelberg Germany 6Institut fur Pathologie Charite Humboldt Universitat Berlin Germany We have investigated the consequences of introducing a bisecting GlcNAc moiety into biantennary N-glycans. Computational analysis of glycan conformation with prolonged simulation periods in vacuo and in a solvent box revealed two main effects backfolding of the a1-6 arm and stacking of the bisecting GlcNAc and the neighboring Man GlcNAc residues of both antennae. Chemoen ymaiic yni-thesis produced the bisecting biantennary decasaccharide N-glycan and its a2-3 6 -sialylated variants. Th v were conjugated to BSA to probe the ligand properties of N-glycans with bisecting GlcNAc. To aseess alììni ty akera-tions in glycan binding to receptors testing was performed with purified lectins cultured cells tissue sections and animals. The pnnel o l leciins. in i g en adhesion growlh-regulatory galectin revealed up to a sixfold difference in affinity constants for these neoglycoproteins relative to data on the unsubstituted glycans reported previously Andre S. Unverzagt C. Kojjma S.-Donn. X. Fmk c. Kk s si K. Gabius H.-J. 1997 Bioconjugate Chem. 8 845-855 . The enhanced affinity .
