Interactions between biomolecules serve as key triggers for many biological processes and, therefore, provide perfect targets for drug discoveries. Biological binding interactions are a dynamic process driven by changes to the environment. Therefore, techniques used to characterize these interactions needs to mirror the level of biological complexity in order to fully understand these systems.
Commonly used label-free binding analysis platforms include Bio-Layer Interferometry (BLI), Surface Plasmon Resonance (SPR), Isothermal Titration Calorimetry (ITC) and Microscale Thermophoresis (MST). In this e-book, the four technologies are compared in terms of their capabilities and workflows to provide guidance for choosing the most suitable platform based on assay needs and application.
Key attributes such as throughput, sample capacity, unattended runtimes, affinity ranges, sensitivity, type of sample matrix and ease of use are important considerations when choosing a biosensor platform to suit your application and workflow needs.
Both the Octet BLI and Pioneer SPR platforms are capable of characterizing a wide range of biomolecular interactions. Pioneer SPR systems are ideal for small molecule and fragment screening workflows (> 70 Da) due to their exquisite sensitivity and next-generation injection capabilities. Octet BLI platforms can be used for analytes > 150 Da and applications involving larger molecular weight analytes such as viruses, nanoparticles, liposomes, and cells.
Octet systems are microfluidics-free providing an essential tool for routine analysis of crude lysates or complex matrices. Crude sample compatibility is useful especially in epitope binning, quantitation, off rate ranking or large screening assays where sample purification is neither required or feasible for efficient workflows.