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Surface Plasmon Resonance: A biosensing technique in which biomolecules capable of binding to specific analytes or ligands are first immobilized on one side of a metallic film. Light is then focused on the opposite side of the film to excite the surface plasmons, that is, the oscillations of free electrons propagating along the film's surface. The refractive index of light reflecting off this surface is measured. When the immobilized biomolecules are bound by their ligands, an alteration in surface plasmons on the opposite side of the film is created which is directly proportional to the change in bound, or adsorbed, mass. Binding is measured by changes in the refractive index. The technique is used to study biomolecular interactions, such as antigen-antibody binding.

Surface Plasmon Resonance (SPR)

JoVE 5697

Surface plasmon resonance (SPR) is the underlying optical phenomenon behind label-free biosensors to evaluate the molecular affinity, kinetics, specificity, and concentration of biomolecules. In SPR, biomolecular interactions occur on a biosensor made of a thin layer of metal on a prism. Real-time interactions of biomolecules can be monitored by measuring the changes of light reflected off the underside of the metal. This video describes the basic concepts of SPR and how it is used to analyze and visualize biomolecular interactions. This is followed by a sample preparation and experimental protocol for investigating binding rates using SPR. In the applications section, SPR imaging, localized SPR, and quantum dot enhanced SPR are explored. Surface plasmon resonance, or SPR, is the underlying phenomenon behind certain label-free biosensors for evaluating binding and adsorption interactions of biomolecules. Binding assays that require labeling, such as ELISA, can be a time-consuming process, and may alter the functionality of the analyte. In SPR, biomolecular interactions occur on a special sensor made of a thin layer of metal on one face of a prism. By monitoring the changes in light reflected off of the underside of the metal, SPR instruments visualize these interactions in real-time without the use of labels. This video


 Biochemistry

Using Extraordinary Optical Transmission to Quantify Cardiac Biomarkers in Human Serum

1NUS Nanoscience and Nanotechnology Initiative, National University of Singapore, 2Cardiovascular Research Institute, Yong Loo Lin School of Medicine, National University of Singapore, 3Department of Electrical and Computer Engineering, National University of Singapore, 4Institute of Materials Research Engineering, A*STAR (Agency for Science, Technology and Research)

JoVE 55597


 Bioengineering

Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens

1Division of Infection and Immunity and Systems Immunity Research Institute, Cardiff University, 2Department of Oncology, University Hospital of Lausanne (CHUV), 3Ludwig Insitutue for Cancer Research, Lausanne Branch, University of Lausanne

JoVE 54991


 Immunology and Infection

Regeneration of Arrayed Gold Microelectrodes Equipped for a Real-Time Cell Analyzer

1School of Public Health, Nanjing Medical University, 2School of Pharmacy, Nanjing Medical University, 3State Key Laboratory of Materials-Oriented Chemical Engineering, College of Chemistry and Chemical Engineering, Nanjing Tech University, 4Department of Medical Oncology, Jiangsu Cancer Hospital, Nanjing Medical University

Video Coming Soon

JoVE 56250


 JoVE In-Press

Towards Biomimicking Wood: Fabricated Free-standing Films of Nanocellulose, Lignin, and a Synthetic Polycation

1Institute for Critical Technology and Applied Science, Virginia Tech, 2Macromolecules and Interfaces Institute, Virginia Tech, 3Institute for Food Safety and Health, Illinois Institute of Technology- Moffett Campus, 4Wood, Cellulose, and Paper Research Department, University of Guadalajara, 5Department of Sustainable Biomaterials, Virginia Tech, 6Sustainable Nanotechnology Interdisciplinary Graduate Education Program, Virginia Tech

JoVE 51257


 Chemistry

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