Affinity analysis of lectin interaction with immobilized C- and O-gylcosides studied by surface plasmon resonance assay
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/331984
- author
- Nahalkova, J ; Svitel, Juraj LU ; Gemeiner, P ; Danielsson, Bengt LU ; Pribulova, B and Petrus, L
- organization
- publishing date
- 2002
- 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}}, }