Carbohydrate–protein interactions at interfaces: comparison of the binding of Ricinus communis lectin to two series of synthetic glycolipids using surface plasmon resonance studies

2003 ◽  
Vol 1 (23) ◽  
pp. 4148-4159 ◽  
Author(s):  
P. Critchley ◽  
G. J. Clarkson
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interactions ◽  
Plasmon Resonance ◽  
Ricinus Communis ◽  
Ricinus Communis Lectin

scholarly journals Use of a Surface Plasmon Resonance Method To Investigate Antibiotic and Plasma Protein Interactions

2009 ◽  
Vol 53 (4) ◽  
pp. 1528-1531 ◽  
Author(s):  
Françoise Banères-Roquet ◽  
Maxime Gualtieri ◽  
Philippe Villain-Guillot ◽  
Martine Pugnière ◽  
Jean-Paul Leonetti
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interactions ◽  
Plasmon Resonance ◽  
Serum Proteins ◽  
Resonance Method ◽  
Pharmacologic Effect ◽  
Nonspecific Interactions ◽  
Automatic Tool ◽  
Hit Validation

ABSTRACT The pharmacologic effect of an antibiotic is directly related to its unbound concentration at the site of infection. Most commercial antibiotics have been selected in part for their low propensity to interact with serum proteins. These nonspecific interactions are classically evaluated by measuring the MIC in the presence of serum. As higher-throughput technologies tend to lose information, surface plasmon resonance (SPR) is emerging as an informative medium-throughput technology for hit validation. Here we show that SPR is a useful automatic tool for quantification of the interaction of model antibiotics with serum proteins and that it delivers precise real-time kinetic data on this critical parameter.

scholarly journals Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions

2013 ◽  
Vol 24 (7) ◽  
pp. 883-886 ◽  
Author(s):  
Robert V. Stahelin
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interactions ◽  
Plasmon Resonance ◽  
Dissociation Rate ◽  
Biomolecular Interactions ◽  
Protein Protein Interactions ◽  
Interaction Kinetics ◽  
Lipid Protein Interactions ◽  
Dissociation Rate Constants

Surface plasmon resonance (SPR) is a powerful technique for monitoring the affinity and selectivity of biomolecular interactions. SPR allows for analysis of association and dissociation rate constants and modeling of biomolecular interaction kinetics, as well as for equilibrium binding analysis and ligand specificity studies. SPR has received much use and improved precision in classifying protein–protein interactions, as well as in studying small-molecule ligand binding to receptors; however, lipid–protein interactions have been underserved in this regard. With the field of lipids perhaps the next frontier in cellular research, SPR is a highly advantageous technique for cell biologists, as newly identified proteins that associate with cellular membranes can be screened rapidly and robustly for lipid specificity and membrane affinity. This technical perspective discusses the conditions needed to achieve success with lipid–protein interactions and highlights the unique lipid–protein interaction mechanisms that have been elucidated using SPR. It is intended to provide the reader a framework for quantitative and confident conclusions from SPR analysis of lipid–protein interactions.

Analysis of protein interactions on protein arrays by a wavelength interrogation-based surface plasmon resonance biosensor

PROTEOMICS ◽  
2004 ◽  
Vol 4 (11) ◽  
pp. 3468-3476 ◽  
Author(s):  
Jong Seol Yuk ◽  
Se-Hui Jung ◽  
Jae-Wan Jung ◽  
Duk-Geun Hong ◽  
Jeong-A Han ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interactions ◽  
Plasmon Resonance ◽  
Protein Arrays ◽  
Surface Plasmon Resonance Biosensor
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