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Surface plasmon resonance for real-time study of lectin-carbohydrate interactions for the differentiation and identification of glycoproteins.

Safina, Gulnara LU ; Duran, Iu Benet; Alasel, Mohammed and Danielsson, Bengt LU (2011) In Talanta 84(5). p.1284-1290
Abstract
A study of specific interactions between lectins and glycoproteins has been carried out using surface plasmon resonance (SPR) in a flow-injection mode. Lectins were covalently immobilised on the surfaces of the microfluidic sensor chip via amine coupling and serum glycoproteins were injected into the flow channels. Specific lectin-glycoprotein interactions caused the shift of refractive index proportional to the mass concentration accumulated on the channel surface. Lectins showed different affinity to the tested glycoproteins and each glycoprotein displayed its own lectin-binding pattern. It is possible to distinguish and identify even glycoproteins with similar sugar structures by simple and quick screening. The working conditions of the... (More)
A study of specific interactions between lectins and glycoproteins has been carried out using surface plasmon resonance (SPR) in a flow-injection mode. Lectins were covalently immobilised on the surfaces of the microfluidic sensor chip via amine coupling and serum glycoproteins were injected into the flow channels. Specific lectin-glycoprotein interactions caused the shift of refractive index proportional to the mass concentration accumulated on the channel surface. Lectins showed different affinity to the tested glycoproteins and each glycoprotein displayed its own lectin-binding pattern. It is possible to distinguish and identify even glycoproteins with similar sugar structures by simple and quick screening. The working conditions of the assay were optimised. The lectin-based SPR made it possible to carry out the label-free detection of glycoproteins within a broad concentration range with a good linearity. Regeneration conditions for the surface of the sensor chip were found and optimised. Combination of 10mM HCl and 10mM glycine-HCl (pH 2.5) removes the bound glycoproteins from the lectin surface without damaging it. The kinetic and affinity parameters of lectin-glycoprotein binding were evaluated. The proposed method was tested on human glycosylated serum. Combination of the lectin panel with SPR is suitable both for specific screening and for sensitive assay of serum glycoproteins. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Talanta
volume
84
issue
5
pages
1284 - 1290
publisher
Elsevier
external identifiers
  • wos:000292475600015
  • pmid:21641439
  • scopus:79958087802
ISSN
1873-3573
DOI
10.1016/j.talanta.2011.01.030
language
English
LU publication?
yes
id
4017c386-61b1-4390-bb3d-8ced1bbb8f46 (old id 2008522)
date added to LUP
2011-07-20 12:07:07
date last changed
2017-10-29 03:59:01
@article{4017c386-61b1-4390-bb3d-8ced1bbb8f46,
  abstract     = {A study of specific interactions between lectins and glycoproteins has been carried out using surface plasmon resonance (SPR) in a flow-injection mode. Lectins were covalently immobilised on the surfaces of the microfluidic sensor chip via amine coupling and serum glycoproteins were injected into the flow channels. Specific lectin-glycoprotein interactions caused the shift of refractive index proportional to the mass concentration accumulated on the channel surface. Lectins showed different affinity to the tested glycoproteins and each glycoprotein displayed its own lectin-binding pattern. It is possible to distinguish and identify even glycoproteins with similar sugar structures by simple and quick screening. The working conditions of the assay were optimised. The lectin-based SPR made it possible to carry out the label-free detection of glycoproteins within a broad concentration range with a good linearity. Regeneration conditions for the surface of the sensor chip were found and optimised. Combination of 10mM HCl and 10mM glycine-HCl (pH 2.5) removes the bound glycoproteins from the lectin surface without damaging it. The kinetic and affinity parameters of lectin-glycoprotein binding were evaluated. The proposed method was tested on human glycosylated serum. Combination of the lectin panel with SPR is suitable both for specific screening and for sensitive assay of serum glycoproteins.},
  author       = {Safina, Gulnara and Duran, Iu Benet and Alasel, Mohammed and Danielsson, Bengt},
  issn         = {1873-3573},
  language     = {eng},
  number       = {5},
  pages        = {1284--1290},
  publisher    = {Elsevier},
  series       = {Talanta},
  title        = {Surface plasmon resonance for real-time study of lectin-carbohydrate interactions for the differentiation and identification of glycoproteins.},
  url          = {http://dx.doi.org/10.1016/j.talanta.2011.01.030},
  volume       = {84},
  year         = {2011},
}