Surface plasmon resonance has several main applications area's. These are listed in the submenu below. In this section applications which fall outside the categories.
Richalet-Secordel, P. M. et al. Concentration measurement of unpurified proteins using biosensor technology under conditions of partial mass transport limitation. Analytical Biochemistry249: 165-173; (1997).
Concentration measurements of non-purified proteins. At high ligand concentration the mass transport is high and binding between ligand and analyte becomes proportional to the analyte concentration. With injections at different flow rates and the analyte molecular weight and diffusion constant it is possible to calculate the analyte concentration without a calibration curve.
Webster, C. I. et al. Kinetic analysis of high-mobility-group proteins HMG-1 and HMG-I/Y binding to cholesterol-tagged DNA on a supported lipid monolayer. Nucleic Acids Res.28: 1618-1624; (2000).
Kinetic analysis of DNA binding proteins with cholesterol-tagged DNA on a supported lipid monolayer. Because High-Mobility-Group proteins react with the dextran matrix a novel method is used to capture DNA. The supported lipid mono layer is almost neutral providing a low binding surface for the HMG-proteins.
Ciolkowski, M. L. et al. A surface plasmon resonance method for detecting multiple modes of DNA-ligand interactions. J.Pharm.Biomed.Anal.22: 1037-1045; (2000). Goto reference.
A surface plasmon resonance method for detecting multiple modes of DNA-ligand interactions. A simple and general surface plasmon resonance (SPR) based method has been developed to detect and quantitate binding of low molecular weight compounds (200-1,200 Da) to double stranded DNA. Several compounds were chosen to probe three different modes of binding interactions, intercalation, minor groove binding and electrostatic interactions.
Gambari, R. et al. Biospecific interaction analysis (BIA) of low-molecular weight DNA-binding drugs. J.Pharmacol.Exp.Ther.294: 370-377; (2000). Goto reference.
Biospecific interaction analysis (BIA) of low-molecular weight DNA-binding drugs. It is demonstrate that molecular interactions between DNA-binding drugs (chromomycin, mithramycin, distamycin, and MEN 10567) and biotinylated target DNA probes immobilized on sensor chips is detectable by SPR technology using a commercially available biosensor.
Svedhem, S. et al. Subtle Differences in Dissociation Rates of Interactions between Destabilized Human Carbonic Anhydrase II Mutants and Immobilized Benzenesulfonamide Inhibitors Probed by a Surface Plasmon Resonance Biosensor. Analytical Biochemistry296: 188-196; (2001).
Kinetic analysis of mutant proteins. The investigation of the subtle kinetic changes in a protein when point mutations are made.
Karlsson, R.. Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface-immobilized receptors. Analytical Biochemistry221: 142-151; (1994).
Competitive kinetic analysis of the interaction between LMW-ligands in solution and surface immobilized receptors. A low molecular weight analyte (<5000 Da) competes with a high molecular analyte for binding to immobilized receptor this method makes it possible do affinity ranking and calculation of the rate constants both low weight analytes.