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

J Nahalkova; Juraj Svitel; P Gemeiner; Bengt Danielsson; B Pribulova; L Petrus

doi:10.1016/S0165-022X(02)00016-7

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

J Nahalkova, Juraj Svitel, P Gemeiner, Bengt Danielsson, B Pribulova, L Petrus

Pure and Applied Biochemistry

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	11-18
Journal	Journal of Biochemical and Biophysical Methods
Volume	52
Issue number	1
DOIs	https://doi.org/10.1016/S0165-022X(02)00016-7
Publication status	Published - 2002

Subject classification (UKÄ)

Biological Sciences

Free keywords

p-aminophenyl
glycosylmethylamine
kinetics
biosensor
lectin
surface plasmon resonance
p-aminophenyl glycoside

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10.1016/S0165-022X(02)00016-7

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

abstract = "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.",

keywords = "p-aminophenyl, glycosylmethylamine, kinetics, biosensor, lectin, surface plasmon resonance, p-aminophenyl glycoside",

author = "J Nahalkova and Juraj Svitel and P Gemeiner and Bengt Danielsson and B Pribulova and L Petrus",

year = "2002",

doi = "10.1016/S0165-022X(02)00016-7",

language = "English",

volume = "52",

pages = "11--18",

journal = "Journal of Biochemical and Biophysical Methods",

issn = "0165-022X",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Affinity analysis of lectin interaction with immobilized C- and O-gylcosides studied by surface plasmon resonance assay

AU - Nahalkova, J

AU - Svitel, Juraj

AU - Gemeiner, P

AU - Danielsson, Bengt

AU - Pribulova, B

AU - Petrus, L

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

KW - p-aminophenyl

KW - glycosylmethylamine

KW - kinetics

KW - biosensor

KW - lectin

KW - surface plasmon resonance

KW - p-aminophenyl glycoside

U2 - 10.1016/S0165-022X(02)00016-7

DO - 10.1016/S0165-022X(02)00016-7

M3 - Article

SN - 0165-022X

VL - 52

SP - 11

EP - 18

JO - Journal of Biochemical and Biophysical Methods

JF - Journal of Biochemical and Biophysical Methods

IS - 1

ER -

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

Abstract

Subject classification (UKÄ)

Free keywords

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