Affinity analysis of lectin interaction with immobilized C- and O- gylcosides studied by surface plasmon resonance assay.
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.
Nahálková
Jarmila
J
Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84238, Bratislava, Slovak Republic.
Svitel
Juraj
J
Gemeiner
Peter
P
Danielsson
Bengt
B
Pribulová
Bozena
B
Petrus
Ladislav
L
D001703:Biophysics / Q000379:methods*; D015374:Biosensing Techniques; D003208:Concanavalin A / Q000494:pharmacology; D006027:Glycosides / Q000737:chemistry*; D006031:Glycosylation; D007700:Kinetics; D037102:Lectins / Q000737:chemistry*; D008024:Ligands; D008956:Models, Chemical; D020349:Surface Plasmon Resonance; D013997:Time Factors
D006027:Glycosides; D037102:Lectins; D008024:Ligands; D003208:Concanavalin A