Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions
Open Access
- 1 April 2013
- journal article
- Published by American Society for Cell Biology (ASCB) in Molecular Biology of the Cell
- Vol. 24 (7), 883-886
- https://doi.org/10.1091/mbc.e12-10-0713
Abstract
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.Keywords
This publication has 15 references indexed in Scilit:
- Curvature, Lipid Packing, and Electrostatics of Membrane Organelles: Defining Cellular Territories in Determining SpecificityDevelopmental Cell, 2012
- Conditional Peripheral Membrane Proteins: Facing up to Limited SpecificityStructure, 2012
- Determining selectivity of phosphoinositide-binding domainsMethods, 2006
- Membrane-Protein Interactions in Cell Signaling and Membrane TraffickingAnnual Review of Biophysics and Biophysical Chemistry, 2005
- Phosphatidylinositol-(4,5)-Bisphosphate Regulates Sorting Signal Recognition by the Clathrin-Associated Adaptor Complex AP2Molecular Cell, 2005
- High-Resolution and High-Throughput Protocols for Measuring Drug/Human Serum Albumin Interactions Using BIACOREAnalytical Biochemistry, 2001
- Characterization of the Surfaces Generated by Liposome Binding to the Modified Dextran Matrix of a Surface Plasmon Resonance Sensor ChipAnalytical Biochemistry, 2000
- [13] Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensorsMethods in Enzymology, 1998
- Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensorsCurrent Opinion in Biotechnology, 1997
- Notizen: Radiative Decay of Non Radiative Surface Plasmons Excited by LightZeitschrift für Naturforschung A, 1968