期刊
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS
卷 52, 期 1, 页码 11-18出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0165-022X(02)00016-7
关键词
lectin; surface plasmon resonance; biosensor; kinetics; glycosylmethylamine; p-aminophenyl; p-aminophenyl glycoside
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. (C) 2002 Elsevier Science B.V. All rights reserved.
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