Surface Plasmon Resonance Spectroscopy: A Versatile Technique in a Biochemist’s Toolbox
Citations Over Time
Abstract
Surface plasmon resonance (SPR) spectroscopy is a powerful, label-free technique to monitor noncovalent molecular interactions in real time and in a noninvasive fashion. As a label-free assay, SPR does not require tags, dyes, or specialized reagents (e.g., enzymes–substrate complexes) to elicit a visible or a fluorescence signal. During the last two decades, SPR has been broadly applied to study of noncovalent interactions of protein–DNA, protein–cell, RNA–DNA, DNA–DNA, protein–protein, protein–carbohydrate, small molecule–macromolecule (e.g., receptor–inhibitor complex), protein–peptide, and self-assembled monolayers. In addition, SPR has been successfully applied to drug discovery ligand-fishing and clinical immunogenicity studies (i.e., to monitor an immune response against a therapeutic agent). SPR spectroscopy can address questions such as specificity of an interaction, kinetics, affinity, and concentrations of selected molecules present in a sample of interest. Given the current enhancements in hardware and software capabilities along with its ease of use and maintenance, SPR experiments can be designed for upper-level undergraduate biochemistry, biophysics, and physical chemistry laboratory courses. In this article, an overview of SPR phenomenon, instrumentation, sensor immobilization, and its selected applications is presented.
Related Papers
- → Stimuli-responsive hydrogel–silver nanoparticles composite for development of localized surface plasmon resonance-based optical biosensor(2008)126 cited
- → Construction of biosensors using a gold-binding polypeptide and a miniature integrated surface plasmon resonance sensor(1998)68 cited
- → Facile Characterization of Aptamer Kinetic and Equilibrium Binding Properties Using Surface Plasmon Resonance(2014)30 cited
- Application of long-range surface plasmon for sensitive detection of Human E.coli(2011)
- Advance in Aptamer-based Biosensors(2011)