Related Experiment Video
Updated: Sep 16, 2025

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors
Published on: April 13, 2019
Human Milk Oligosaccharides Multivalently Presented on Defined Synthetic Neo-Glycoproteins Are Nanomolar Ligands of
Jakub Červený1,2, Viktoria Heine1, Michaela Hovorková1,3
1Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ-142 00 Prague 4, Czech Republic.
Abstract:
Galectins are small human proteins participating in inflammation processes, immune response, and cancerogenesis. Tandem-repeat galectins comprising Gal-4, Gal-8, and Gal-9 are a vital yet less studied part of the galectin fingerprint in cancer-related processes. The present work studies a library of prepared multivalent neo-glycoproteins decorated with poly-N-acetyllactosamine and human-milk-type oligosaccharides as ligands of this underexplored family of tandem-repeat galectins. A thorough binding evaluation by ELISA and biolayer interferometry was complemented with a detailed epitope mapping both from the galectin and the glycoconjugate viewpoints by nuclear magnetic resonance. The found interactions in the galectin binding site were correlated to in silico data from molecular modeling. The present work reveals pioneer information on the binding of tandem-repeat galectins to multivalent glycoconjugates carrying complex carbohydrate ligands and represents an invaluable starting point for the development of new high-affinity tailored ligands of tandem-repeat galectins, needed both for diagnosis and therapy.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Proteoglycans
Protein Glycosylation
Glycosylation occurs in...
Matrix Proteoglycans and Glycoproteins

