Title: Biacore T200 Surface Plasmon Resonance Spectroscopy Surface plasmon resonance (SPR) spectroscopy is a powerful instrument to measure biomolecular interactions in real-time and a label free environment. SPR has been applied to characterize the binding events with samples ranging from proteins, nucleic acids, carbohydrates, small molecules to complex mixtures, lipid vesicles, viruses, bacteria, and eukaryotic cells. This project is a Shared Instrumentation Grant Program (S10) application entitled ?Biacore T200 Surface Plasmon Resonance Spectroscopy?. The Biacore T200 is a versatile, label-free system for detailed studies of biomolecular interactions delivering high quality kinetic, affinity and thermodynamic interaction data in real time with exceptional sensitivity. The system will be very useful in fundamental biological studies, health/clinic science research, drug discovery, environmental and biopharmaceutical process monitoring for large groups of researchers in our Center for Biotechnology & Interdisciplinary Studies (CBIS). A Biacore 3000 instrument currently housed in CBIS has reached the end of its useful life with the discontinuation of this instrument model. This instrument was used in over 100 research studies examining protein-protein, protein- glycan, glycan-glycan, protein-lipid, protein-DNA, DNA-DNA, protein-nanoparticle interactions published by CBIS faculty from 2004-2019. Many CBIS research groups will use the more sensitive and higher throughput Biacore T200 SPR to study the molecular interactions with important physiological significance in signaling and developmental biology and pathophysiological significance, including ones related to cancer, kidney disease, infectious disease, and Alzheimer?s disease. The data from SPR analysis will provide a deeper understanding of many of the biochemical pathways and networks.
This project is a Shared Instrumentation Grant Program application entitled ?Biacore T200 Surface Plasmon Resonance Spectroscopy?. The Biacore T200 is a versatile, label-free system for detailed studies of biomolecular (such as protein-protein, protein-DNA, protein-glycan, protein-lipid, and other ligands) interactions delivering high quality kinetic, affinity and thermodynamic interaction data in real time with exceptional sensitivity.
