A strategy for analyzing bond strength and interaction kinetics between Pleckstrin homology domains and PI(4,5)P2 phospholipids using force distance spectroscopy and surface plasmon resonance

The Analyst ◽  
2015 ◽  
Vol 140 (13) ◽  
pp. 4558-4565 ◽  
Author(s):  
A. V. Malkovskiy ◽  
D. A. Wagh ◽  
F. M. Longo ◽  
J. Rajadas
Keyword(s):  
Surface Plasmon Resonance ◽  
Bond Strength ◽  
Surface Plasmon ◽  
Single Molecule ◽  
Plasmon Resonance ◽  
Protein Domains ◽  
Pleckstrin Homology ◽  
Interaction Kinetics ◽  
Homology Domains

Use of AFM force–distance spectroscopy and SPR analysis to assess strong single-molecule binding between PH protein domains and phosphatidylinositol phospholipids.

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.

A single molecule immunoassay by localized surface plasmon resonance

2010 ◽  
Vol 21 (25) ◽  
pp. 255503 ◽  
Author(s):  
Kathryn M Mayer ◽  
Feng Hao ◽  
Seunghyun Lee ◽  
Peter Nordlander ◽  
Jason H Hafner
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Single Molecule ◽  
Plasmon Resonance ◽  
Localized Surface Plasmon Resonance ◽  
Localized Surface Plasmon

Insulin receptor-insulin interaction kinetics using multiplex surface plasmon resonance

2013 ◽  
Vol 26 (12) ◽  
pp. 643-652 ◽  
Author(s):  
Kannan Subramanian ◽  
Conan J. Fee ◽  
Rayleen Fredericks ◽  
Richard S. Stubbs ◽  
Mark T. Hayes
Keyword(s):  
Surface Plasmon Resonance ◽  
Insulin Receptor ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Interaction Kinetics

scholarly journals Single molecule interactions studied by using a modified DNA sequencer: a comparison with surface plasmon resonance

2013 ◽  
Author(s):  
Jens Sobek ◽  
Stefan Schauer ◽  
Hubert Rehrauer ◽  
David Fischer ◽  
Andrea Patrignani ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Single Molecule ◽  
Plasmon Resonance ◽  
Modified Dna ◽  
Molecule Interactions ◽  
Dna Sequencer

Interaction kinetics of salmeterol with egg phosphatidylcholine liposomes by surface plasmon resonance

2009 ◽  
Vol 385 (2) ◽  
pp. 215-223 ◽  
Author(s):  
Dario Lombardi ◽  
Bernard Cuenoud ◽  
Heidi Wunderli-Allenspach ◽  
Stefanie D. Krämer
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Phosphatidylcholine Liposomes ◽  
Interaction Kinetics ◽  
Kinetics Of
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