Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology.
The review gives first an introduction into the basics of surface plasmon resonance technology. The physical principle is shortly discussed followed by a discussion of the experimental details to be considered when using this technology for biomolecular interaction analysis. Based on recent publications it is demonstrated that the technology has widespread applications in many fields of the drug discovery process. Protein/protein interactions can be monitored in real time when working with biopharmaceuticals as well as protein/small analyte interactions during hit finding, secondary screening, lead optimization and lead selection. Equilibrium binding constants, kinetic rate constants and thermodynamic parameters are obtained from such study that helps to understand the mechanism of the binding reactions. This information can be directly used to improve binding properties of a drug candidate.
Huber
Walter
W
F. Hoffmann-La Roche AG, Department of Pharma Research, CH-4070 Basel, Switzerland. walter.huber@roche.com
Mueller
Francis
F
D000911:Antibodies, Monoclonal / Q000737:chemistry / Q000378:metabolism; D015195:Drug Design; D007700:Kinetics; D008024:Ligands; D015394:Molecular Structure; D004364:Pharmaceutical Preparations / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D020349:Surface Plasmon Resonance / Q000295:instrumentation / Q000379:methods; D013816:Thermodynamics
D000911:Antibodies, Monoclonal; D008024:Ligands; D004364:Pharmaceutical Preparations; D011506:Proteins