Affinity analysis of lectin interaction with immobilized C- and O-gylcosides studied by surface plasmon resonance assay

被引：23
作者：
Nahálková, J
Svitel, J
Gemeiner, P
Danielsson, B
Pribulová, B
Petrus, L
机构：
[1] Slovak Acad Sci, Inst Chem, SK-84238 Bratislava, Slovakia
[2] Lund Univ, Ctr Chem, S-22100 Lund, Sweden
来源：
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS | 2002年 / 52卷 / 01期
关键词：
lectin; surface plasmon resonance; biosensor; kinetics; glycosylmethylamine; p-aminophenyl; p-aminophenyl glycoside;
D O I：
10.1016/S0165-022X(02)00016-7
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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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收藏
页码：11 / 18
页数：8
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