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Affinity analysis of lectin interaction with immobilized C- and O- gylcosides studied by surface plasmon resonance assay
Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84238, Bratislava, Slovak Republic.
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2002 (English)In: Journal of Biochemical and Biophysical Methods, ISSN 0165-022X, E-ISSN 1872-857X, Vol. 52, no 1, 11-18 p.Article in journal (Refereed) Published
Abstract [en]

A biosensor based on the surface plasmon resonance (SPR) principle was used for kinetic analysis of lectin interactions with different immobilized saccharide structures. A novel affinity ligands beta-D-glycopyranosylmethylamines derived from common D-aldohexoses linked to the carboxymethyl dextran layer of the SPR sensor surface served for interactions with a wide range of lectins. The method of preparation and use of the beta-D-mannopyranosyl glycosylated sensor surface was described. The results of affinity analysis of lectin-ligand interactions were evaluated and compared with data obtained from measurements using commercially available p-aminophenyl alpha-D-glycopyranosides. Possible applications and advantages of C- and O-glycosylated SPR biosensors are discussed.

Place, publisher, year, edition, pages
2002. Vol. 52, no 1, 11-18 p.
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Biological Sciences
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URN: urn:nbn:se:uu:diva-216575DOI: 10.1016/S0165-022X(02)00016-7PubMedID: 12121750OAI: oai:DiVA.org:uu-216575DiVA: diva2:690365
Available from: 2014-01-23 Created: 2014-01-23 Last updated: 2017-12-06Bibliographically approved

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Nahálková, Jarmila

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