Characterization of the Carbohydrate Binding Specificity and Kinetic Parameters of Lectins by Using Surface Plasmon Resonance

1999 ◽  
Vol 274 (2) ◽  
pp. 203-210 ◽  
Author(s):  
Simon R. Haseley ◽  
Philippe Talaga ◽  
Johannis P. Kamerling ◽  
Johannes F.G. Vliegenthart
Keyword(s):  
Surface Plasmon Resonance ◽  
Kinetic Parameters ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Specificity ◽  
Carbohydrate Binding

Analysis of the carbohydrate binding specificity of the mushroom Pleurotus ostreatus lectin by surface plasmon resonance

2005 ◽  
Vol 336 (1) ◽  
pp. 87-93 ◽  
Author(s):  
Yuka Kobayashi ◽  
Hiroko Nakamura ◽  
Takehiko Sekiguchi ◽  
Ryo Takanami ◽  
Takeomi Murata ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Pleurotus Ostreatus ◽  
Binding Specificity ◽  
Carbohydrate Binding

scholarly journals Determination of the composition of heterogeneous binder solutions by surface plasmon resonance biosensing

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jimmy Gaudreault ◽  
Benoît Liberelle ◽  
Yves Durocher ◽  
Olivier Henry ◽  
Gregory De Crescenzo
Keyword(s):  
Surface Plasmon Resonance ◽  
Data Analysis ◽  
Kinetic Parameters ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Total Concentration ◽  
Accurate Determination ◽  
Small Molecular Weight

AbstractSurface plasmon resonance-based biosensors have been extensively applied to the characterization of the binding kinetics between purified (bio)molecules, thanks to robust data analysis techniques. However, data analysis for solutions containing multiple interactants is still at its infancy. We here present two algorithms for (1) the reliable and accurate determination of the kinetic parameters of N interactants present at different ratios in N mixtures and (2) the estimation of the ratios of each interactant in a given mixture, assuming that their kinetic parameters are known. Both algorithms assume that the interactants compete to bind to an immobilized ligand in a 1:1 fashion and necessitate prior knowledge of the total concentration of all interactants combined. The effectiveness of these two algorithms was experimentally validated with a model system corresponding to mixtures of four small molecular weight drugs binding to an immobilized protein. This approach enables the in-depth characterization of mixtures using SPR, which may be of considerable interest for many drug discovery or development applications, notably for protein glycovariant analysis.

Characterization of Surface-Confined α-Synuclein by Surface Plasmon Resonance Measurements

Langmuir ◽  
2006 ◽  
Vol 22 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Taewook Kang ◽  
Surin Hong ◽  
Hyun Jin Kim ◽  
Jungwoo Moon ◽  
Seogil Oh ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance

scholarly journals Lectins at Interfaces—An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study

Materials ◽  
2018 ◽  
Vol 11 (12) ◽  
pp. 2348 ◽  
Author(s):  
Katrin Niegelhell ◽  
Thomas Ganner ◽  
Harald Plank ◽  
Evelyn Jantscher-Krenn ◽  
Stefan Spirk
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Plasmon Resonance ◽  
Protein Adsorption ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Resonance Spectroscopy ◽  
Carbohydrate Binding ◽  
Force Microscopy ◽  
Atomic Force ◽  
Slow Kinetics

Lectins are a diverse class of carbohydrate binding proteins with pivotal roles in cell communication and signaling in many (patho)physiologic processes in the human body, making them promising targets in drug development, for instance, in cancer or infectious diseases. Other applications of lectins employ their ability to recognize specific glycan epitopes in biosensors and glycan microarrays. While a lot of research has focused on lectin interaction with specific carbohydrates, the interaction potential of lectins with different types of surfaces has not been addressed extensively. Here, we screen the interaction of two specific plant lectins, Concanavalin A and Ulex Europaeus Agglutinin-I with different nanoscopic thin films. As a control, the same experiments were performed with Bovine Serum Albumin, a widely used marker for non-specific protein adsorption. In order to test the preferred type of interaction during adsorption, hydrophobic, hydrophilic and charged polymer films were explored, such as polystyrene, cellulose, N,-N,-N-trimethylchitosan chloride and gold, and characterized in terms of wettability, surface free energy, zeta potential and morphology. Atomic force microscopy images of surfaces after protein adsorption correlated very well with the observed mass of adsorbed protein. Surface plasmon resonance spectroscopy studies revealed low adsorbed amounts and slow kinetics for all of the investigated proteins for hydrophilic surfaces, making those resistant to non-specific interactions. As a consequence, they may serve as favorable supports for biosensors, since the use of blocking agents is not necessary.

Development and Characterization of a Diamond-Based Localized Surface Plasmon Resonance Interface

2010 ◽  
Vol 114 (8) ◽  
pp. 3346-3353 ◽  
Author(s):  
Sabine Szunerits ◽  
Slimane Ghodbane ◽  
Joanna Niedziółka-Jönsson ◽  
Elisabeth Galopin ◽  
Frederik Klauser ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Localized Surface Plasmon Resonance ◽  
Localized Surface Plasmon

Characterization of labeled reagents in ligand-binding assays by a surface plasmon resonance biosensor

Bioanalysis ◽  
2017 ◽  
Vol 9 (2) ◽  
pp. 193-207 ◽  
Author(s):  
Jia Duo ◽  
JoAnne Bruno ◽  
Steven Piccoli ◽  
Binodh DeSilva ◽  
Yan J Zhang
Keyword(s):  
Surface Plasmon Resonance ◽  
Ligand Binding ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Assays ◽  
Surface Plasmon Resonance Biosensor

scholarly journals Characterization of thermal bump due to surface plasmon resonance

2019 ◽  
Vol 27 (15) ◽  
pp. 21717
Author(s):  
Tsz Kit Yung ◽  
Ranran Zhang ◽  
Qiuling Zhao ◽  
Xia Wang ◽  
Wensheng Gao ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance
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