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Sialic acid and sialyl-lactose glyco-conjugates: design, synthesis and binding assays to lectins and swine influenza H1N1 virus


Stella Zevgiti, Department of Chemistry, Section of Organic Chemistry and Biochemistry, University of Ioannina, 45110 Ioannina, Greece.



The terminal parts of the influenza hemagglutinin (HA) receptors α2,6- and α2,3-sialyllactoses were conjugated to an artificial carrier, named sequential oligopeptide carrier (SOC4), to formulate human and avian receptor mimics, respectively. SOC4, formed by the tripeptide unit Lys-Aib-Gly, adopts a rigid helicoids-type conformation, which enables the conjugation of biomolecules to the Lys-NεH2 groups. By doing so, it preserves their initial conformations and functionalities of the epitopes. We report that SOC4-glyco-conjugate bearing two copies of the α2,6-sialyllactose is specifically recognized by the biotinylated Sambucus nigra (elderberry) bark lectin, which binds preferentially to sialic acid in an α2,6-linkage. SOC4-glyco-conjugate bearing two copies of the α2,3-sialyllactose was not recognized by the biotinylated Maackia amurensis lectin, despite its well-known α2,3-sialyl bond specificity. However, preliminary immune blot assays showed that H1N1 virus binds to both the SOC4-glyco-conjugates immobilized onto nitrocellulose membrane. It is concluded that Ac-SOC4[(Ac)2,(3′SL-Aoa)2]-NH2 5 and Ac-SOC4[(Ac)2,(6′SL-Aoa)2]-NH2 6 mimic the HA receptors. These findings could be useful for easy screening of binding and inhibition assays of virus–receptor interactions. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.