Sialic acid and sialyl-lactose glyco- conjugates: design, synthesis andbinding assays to lectins and swine influenza H1N1 virus (EN)

Zevgiti, S., (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)

Zevgiti, S., (EN)

The terminal parts of the influenza hemagglutinin (HA) receptors Ξ±2,6- and Ξ±2,3-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-NΞµH2 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 Ξ±2,6-sialyllactose is specifically recognized by the biotinylated Sambucus nigra (elderberry) bark lectin, which binds preferentially to sialic acid in an Ξ±2,6-linkage. SOC4-glyco-conjugate bearing two copies of the Ξ±2,3-sialyllactose was not recognized by the biotinylated Maackia amurensis lectin, despite its well-known Ξ±2,3-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. (EN)

Influenza virus (EN)

Πανεπιστήμιο Ιωαννίνων

Ιδρυματικό Αποθετήριο Ολυμπιάς

Σχολή Θετικών Επιστημών

Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"

Τμήμα Χημείας

J. Pept. Sci. (EN)

Αγγλική γλώσσα

2012

http://onlinelibrary.wiley.com/doi/10.1002/psc.1415/abstract

http://olympias.lib.uoi.gr/jspui/handle/123456789/9152

Wiley (EN)