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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 Methods1979-01-01+01:002008-01-01+01:00 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
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 Methods1979-01-01+01:002008-01-01+01:00
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
2007-11-16 11:00:54
date last changed
2017-11-30 16:12:55
@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},
  keyword      = {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 Methods1979-01-01+01:002008-01-01+01:00},
  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},
  volume       = {52},
  year         = {2002},
}