Fingerprints of Calcium-Binding Protein Conformational Dynamics Monitored by Surface Plasmon Resonance

2016 ◽  
Vol 11 (9) ◽  
pp. 2390-2397 ◽  
Author(s):  
Daniele Dell’Orco ◽  
Karl-Wilhelm Koch
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Calcium Binding ◽  
Binding Protein ◽  
Conformational Dynamics ◽  
Calcium Binding Protein ◽  
Protein Conformational Dynamics

scholarly journals Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by Surface Plasmon Resonance (BiaCore)

2011 ◽  
Vol 105 (06) ◽  
pp. 1053-1059 ◽  
Author(s):  
Berhane Ghebrehiwet ◽  
Kusumam Joseph ◽  
Alice Kao ◽  
Khalil Bdeir ◽  
Douglas Cines ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Surface Plasmon Resonance ◽  
Endothelial Cell ◽  
High Molecular Weight ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Proteins ◽  
Binding Protein ◽  
High Molecular Weight Kininogen ◽  
Cell Binding

SummaryThe physiologic activation of the plasma kallikrein-kinin system requires the assembly of its constituents on a cell membrane. High-molecular-weight kininogen (HK) and cleaved HK (HKa) both interact with at least three endothelial cell binding proteins: urokinase plasminogen activator receptor (uPAR), globular C1q receptor (gC1qR,) and cytokeratin 1 (CK1). The affinity of HK and HKa for endothelial cells are KD=7–52 nM. The contribution of each protein is unknown. We examined the direct binding of HK and HKa to the soluble extracellular form of uPAR (suPAR), gC1qR and CK1 using surface plasmon resonance. Each binding protein linked to a CM-5 chip and the association, dissociation and KD (equilibrium constant) were measured. The interaction of HK and HKa with each binding protein was zinc-dependent. The affinity for HK and HKa was gC1qR>CK1>suPAR, indicating that gC1qR is dominant for binding. The affinity for HKa compared to HK was the same for gC1qR, 2.6-fold tighter for CK1 but 53-fold tighter for suPAR. Complex between binding proteins was only observed between gC1qR and CK1 indicating that a binary CK1-gC1qR complex can form independently of kininogen. Although suPAR has the weakest affinity of the three binding proteins, it is the only one that distinguished between HK and HKa. This finding indicates that uPAR may be a key membrane binding protein for differential binding and signalling between the cleaved and uncleaved forms of kininogen. The role of CK1 and gC1qR may be to initially bind HK to the membrane surface before productive cleavage to HKa.

scholarly journals Determination of Vitamin B12 in Fortified Bovine Milk- Based Infant Formula Powder, Fortified Soya-Based Infant Formula Powder, Vitamin Premix, and Dietary Supplements by Surface Plasmon Resonance: Collaborative Study

2011 ◽  
Vol 94 (4) ◽  
pp. 1217-1226 ◽  
Author(s):  
Pathik Vyas ◽  
Anthony A O'kane ◽  
E Ager ◽  
S Crooks ◽  
C Elliott ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Protein Binding ◽  
Vitamin B12 ◽  
Infant Formula ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Protein ◽  
Collaborative Study ◽  
Wide Range

Abstract A collaborative study was conducted on an inhibition-based protein-binding assay using the Biacore Q™ biosensor instrument and the Biacore Qflex™ Kit Vitamin B12 PI. The samples studied included infant formula, cereals, premixes, vitamin tablets, dietary supplements, and baby food. The collaborative study, which involved 11 laboratories, demonstrated that the assay showed an RSDr of 1.59–27.8 and HorRat values for reproducibility of 0.34–1.89 in samples with levels ranging from ppm to ppb. The assay studied is a label-free protein binding-based assay that uses the principle of surface plasmon resonance (SPR) to measure the interaction between vitamin B12 and a specifc binding protein. A Biacore Q biosensor uses this principle to detect binding directly at the surface of a sensor chip with a hydrophilic gold-dextran surface. The instrument passes a mixture of prepared sample extract and binding protein solution across a covalently immobilized vitamin B12 chip surface, and the response is given as free-binding protein as the mixture binds to the immobilized surface. This technique uses the specifcity and robustness of the protein-ligand interaction to allow minimal sample preparation and a wide range of matrixes to be analyzed rapidly. The reagents and accessories needed to perform this assay are provided as the ready-to-use format “Qflex Kit Vitamin B12 PI.” The method is intended for routine use in the quantitative determination of vitamin B12 (as cyanocobalamin) in a wide range of food products, dietary vitamin supplements, and multivitamin premixes.

Direct detection of glucose by surface plasmon resonance with bacterial glucose/galactose-binding protein

2004 ◽  
Vol 19 (7) ◽  
pp. 653-660 ◽  
Author(s):  
Helen V Hsieh ◽  
Zachary A Pfeiffer ◽  
Terry J Amiss ◽  
Douglas B Sherman ◽  
J.Bruce Pitner
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Direct Detection ◽  
Binding Protein

Use of surface plasmon resonance in the binding study of vitamin D, metabolites and analogues with vitamin D binding protein

2017 ◽  
Vol 409 (10) ◽  
pp. 2547-2558 ◽  
Author(s):  
Pilar Canoa ◽  
Marcos L. Rivadulla ◽  
Jonathan Popplewell ◽  
René van Oosten ◽  
Generosa Gómez ◽  
...  
Keyword(s):  
Vitamin D ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Protein ◽  
Binding Study ◽  
Vitamin D Metabolites ◽  
Vitamin D Binding Protein

Miniaturized Surface Plasmon Resonance Biosensor for Odorant and Pheromone Detection Using Odorant Binding Protein

2014 ◽  
Vol 12 (6) ◽  
pp. 961-966
Author(s):  
Hui-Chong Lau ◽  
Yeon-Kyung Lee ◽  
Jae-Young Kwon ◽  
Young-Soo Sohn ◽  
Jeung-Soo Huh ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Pheromone Detection ◽  
Surface Plasmon Resonance Biosensor ◽  
Odorant Binding
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