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

Nahalkova, J ; Svitel, Juraj LU ; Gemeiner, P ; Danielsson, Bengt LU ; Pribulova, B and Petrus, L (2002) In Journal of Biochemical and Biophysical Methods 52(1). p.11-18
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... (More)
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. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
p-aminophenyl, glycosylmethylamine, kinetics, biosensor, lectin, surface plasmon resonance, p-aminophenyl glycoside
in
Journal of Biochemical and Biophysical Methods
volume
52
issue
1
pages
11 - 18
publisher
Elsevier
external identifiers
  • wos:000177258700002
  • scopus:0037188894
ISSN
0165-022X
DOI
10.1016/S0165-022X(02)00016-7
language
English
LU publication?
yes
id
cc5b4b2f-92f5-4c6a-b5c9-06e1b9991819 (old id 331984)
date added to LUP
2016-04-01 15:58:43
date last changed
2022-01-28 08:27:53
@article{cc5b4b2f-92f5-4c6a-b5c9-06e1b9991819,
  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.}},
  author       = {{Nahalkova, J and Svitel, Juraj and Gemeiner, P and Danielsson, Bengt and Pribulova, B and Petrus, L}},
  issn         = {{0165-022X}},
  keywords     = {{p-aminophenyl; glycosylmethylamine; kinetics; biosensor; lectin; surface plasmon resonance; p-aminophenyl glycoside}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{11--18}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Biochemical and Biophysical Methods}},
  title        = {{Affinity analysis of lectin interaction with immobilized C- and O-gylcosides studied by surface plasmon resonance assay}},
  url          = {{http://dx.doi.org/10.1016/S0165-022X(02)00016-7}},
  doi          = {{10.1016/S0165-022X(02)00016-7}},
  volume       = {{52}},
  year         = {{2002}},
}