Ligand Immobilization in Protein Interaction Studies — An Unattended Amine Coupling Protocol with Automatic Coinjection Activation
Amine coupling is the most commonly adopted technique to bind proteins to biosensor chips. Because of the possibility of the amine coupling reagents reacting with each other, these have to be premixed just before the injection and injected independently. Here are some tips to automatically coinject these reagents.
Novel Liposome-Capture Surface Chemistries to Analyze Drug-Lipid Interaction Using the ProteOn™ XPR36 System
Surface plasmon resonance (SPR) biosensors offer a label-free technique for profiling biomolecular interactions, including those between drugs and liposomes. Here we describe the novel surface chemistries that make capturing liposomes possible, and explore the application of the liposome capturing kit in analyzing liposome-small molecule interactions.
Can we construct molecules that will interfere with disease pathways? Dan Mitchell of the University of Warwick and his colleagues wanted to apply new synthesis techniques to interrupting HIV infection. Find out what they learned about the potential of these novel molecules using Bio-Rad’s ProteOn™ XPR36 System.
Efficient SPR-Based Fragment Screening and Small Molecule Affinity Analysis Using Bio-Rad’s ProteOn™ XPR36 System
Fragment-based screening has emerged as an important tool for identifying lead compounds in drug discovery, though the molecules involved present challenges related to their low affinity. Label-free surface plasmon resonance (SPR) analysis provides an efficient and reproducible solution to these challenges. Here we describe ways to determine small molecule affinity that combines high sensitivity and high throughput with low sample consumption.
Good data processing practice ensures that protein interaction experiments using a surface plasmon resonance (SPR) system will yield the clearest possible results. Here we present tips for understanding and processing SPR sensorgrams when using Bio-Rad’s ProteOn™ XPR36 protein interaction array system.
Analyzing protein interaction data using a surface plasmon resonance (SPR) system can be complicated. This user guide describes how to analyze SPR data to obtain kinetic and equilibrium constants, as well as sample concentrations.
This appendix to “Guide to SPR Data Analysis on the Proteon™ XPR36 System” gives information on the data set export using ProteOn Manager™ Software.
A Novel Biotinylated Ligand-Capture Method with Surface Regeneration Capability for Label-Free Biomolecular Interaction Analysis
Ligand-capture approaches using biotin as an affinity tag are often utilized in biomolecular interaction analyses with surface plasmon resonance (SPR) biosensors. However, a drawback to using biotin is that it makes surface regeneration of SPR sensor chips difficult. Here is a strategy that facilitates surface regeneration when using biotinylated ligand-capture approaches to SPR analysis.
Surface plasmon resonance (SPR) is a well-established and important screening tool in the small molecule drug discovery workflow. Using the Bio-Rad SPR system ProteOn XPR36, rapid optimization of immobilization conditions for a kinase target was carried out in a fast workflow with a single sensor chip, showing the high performance of the ProteOn XPR36 system.
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.