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.

• MeSH
• galektiny * chemie   metabolismus   MeSH
• glykoproteiny * chemie   metabolismus   MeSH
• lidé MeSH
• ligandy MeSH
• mateřské mléko * chemie   MeSH
• oligosacharidy * chemie   metabolismus   MeSH
• tandemové repetitivní sekvence MeSH
• vazebná místa MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• galektiny * MeSH
• glykoproteiny * MeSH
• ligandy MeSH
• oligosacharidy * MeSH
• poly-N-acetyllactosamine MeSH Prohlížeč
• polysacharidy MeSH