Analyzing Binding Kinetics with Surface Plasmon Resonance Complemented with Direct Mass Spectrometry on the Same Sensor Chip
Surface Plasmon Resonance (SPR) is an optical phenomenon that is used for the label-free analysis of the binding of any two molecules in real-time.
Analyzing antibody binding to histidine-tagged proteins is not always easy because of inherent problems such as nonspecific binding and loss of analyte response associated with these tagged proteins. Optimization of these factors is key to precisely measuring the binding kinetics of these proteins.
Highly Efficient Lipoparticle Capture and SPR Binding Kinetics of a Membrane Protein Using the ProteOn™ XPR36 Protein Interaction Array System
The genes coding for membrane proteins, such as G-protein coupled receptors (GPCR), ion channels, and other membrane-bound enzymes make up 25–30% of the human genome and membrane proteins are estimated to represent 30–40% of the top drug targets. There is growing research, industrial, and commercial interest in the study of membrane proteins in general, and more specifically in immobilizing membrane proteins to various biosensor surfaces.
The HTE sensor chip is designed for label-free biomolecular interaction analysis with polyhistidine-tagged proteins. It features a novel tris-NTA (3-NTA) surface for excellent performance of polyhistidine-tagged protein capture, providing high binding stability and regeneracy. It is an ideal choice for the applications of protein-small molecule and other protein interactions requiring high sensitivity.
The ProteOn XPR36 protein interaction analysis system was introduced in 2006 to provide a novel array technology to researchers conducting label-free analysis of proteins. The ProteOn system is a high-throughput surface plasmon resonance-based screening tool for a wide range of applications from small-molecule drug discovery to antibody kinetic ranking, epitope binning, and epitope mapping.