Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors.
Progress has been made in the identification of experimental and analytical procedures that allow for a more reliable determination of equilibrium and kinetic constants. Possible origins of the frequently observed deviations of the measured binding progress from that expected for chemical binding of pseudo-first order, and appropriate experimental controls have been proposed. Improved analytical approaches include the application of global analysis and analytical corrections for the influence of mass transport.
Schuck
P
P
Biomedical Engineering and Instrumentation Program, National Institutes of Health, Bethesda, MD 20892-5766, USA. pschuck@helix.nih.gov
D001665:Binding Sites; D015374:Biosensing Techniques; D007700:Kinetics; D046911:Macromolecular Substances; D055095:Optics and Photonics; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D046911:Macromolecular Substances; D011506:Proteins