The two Biacore machines in our facility, Biacore T-200 and Biacore 4000, utilize the Surface Plasmon Resonance (SPR) technology to study molecular binding events on a chip surface. The basic principle involves immobilization of a ligand on a sensor chip followed by delivery of an analyte by a microfluidic system. Any protein, DNA, RNA, lipid, carbohydrate, polysaccharide, cell, virus, drug, drug like molecule (organic or inorganic) can be used as the ligand or analyte. Since the detection system is based on measuring total mass on the sensor chip surface neither ligand nor analyte has to be tagged. In addition to identifying binding partners to a target molecule, SPR also provides quantitative data on:
Specificity: How specific is the binding between two molecules?
Concentration: How much of a given molecule is present and active?
Kinetics: What is the rate of association and dissociation?
Affinity: How strong is the binding?
Internal Users: Click here for instrument scheduling.
Users from outside of Georgetown University, please contact us through Science Exchange.
In all publications that include data derived or methods used from the Biacore Molecular Interaction Shared Resource, please acknowledge our resource. Both Biacore T-200 and Biacore 4000 instruments were purchased with support from NIH’s S10 shared instrument grants (1S10OD019982-01 and 1S10RR022388-01). The Biacore Molecular Interaction Shared Resource is partially supported by NIH/NCI grant P30-CA051008.