Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis

J Chromatogr. 1992 Apr 24;597(1-2):397-410. doi: 10.1016/0021-9673(92)80137-j.

Abstract

A system for real-time biospecific interaction analysis using biosensor technology based on the optical phenomenon surface plasmon resonance is described. The biospecific interface is a sensor chip covered with a hydrogel matrix. One component of the interaction to be studied is immobilized covalently to the hydrogel and other interactants are passed over the chip in solution. The mass change at the sensor surface, reflecting the progress of the interaction studied, is monitored in real time. The technique, which does not require molecular labels for detection, can measure mass changes down to 10 pg/mm2. Repeated analyses can be performed on the same sensor chip. Applications shown include kinetic measurements, binding site analysis and concentration determination.

MeSH terms

  • Antibodies, Monoclonal / analysis
  • Base Sequence
  • Binding Sites
  • Biosensing Techniques*
  • Gels
  • Kinetics
  • Molecular Sequence Data
  • Refractometry
  • Surface Properties

Substances

  • Antibodies, Monoclonal
  • Gels