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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Zevgiti, S., | en |
| dc.contributor.author | Gonzalez Zabala, J., | en |
| dc.contributor.author | Darji, A., | en |
| dc.contributor.author | Dietrich, U., | en |
| dc.contributor.author | Panou- Pomonis, E., | en |
| dc.contributor.author | Sakarellos- Daitsiotis, M. | en |
| dc.date.accessioned | 2015-11-24T16:47:13Z | - |
| dc.date.available | 2015-11-24T16:47:13Z | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9152 | - |
| dc.rights | Default Licence | - |
| dc.subject | Influenza virus | en |
| dc.subject | sequential oligopeptide carrier (SOC4) | en |
| dc.subject | chemoselective oxime ligation | en |
| dc.subject | SOC4-sialo-conjugates | en |
| dc.subject | HA-binding receptor mimics | en |
| dc.subject | lectin binding assays | en |
| dc.subject | immune blot binding of H1N1 | en |
| dc.title | Sialic acid and sialyl-lactose glyco- conjugates: design, synthesis andbinding assays to lectins and swine influenza H1N1 virus | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | 10.1002/psc.1415 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/doi/10.1002/psc.1415/abstract | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2012 | - |
| heal.abstract | 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 |
| heal.publisher | Wiley | en |
| heal.journalName | J. Pept. Sci. | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Panou-2012-Sialic acid and.pdf | 233.81 kB | Adobe PDF | View/Open Request a copy |
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