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.
From the origins of digital PCR in leukemia research to stopping HIV with novel polymers to better methods for fragment-based drug discovery, BioRadiations has covered some of the most exciting life science research stories of 2013. Now take a look back at these stories and more as we review the best pieces of the year.
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.
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.
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.