BLI is an optical technique that measures biomolecular interactions in real time. This label-free method eliminates the need for tags or dyes, preserving the natural behavior of your molecules.
BLI uses fiber-optical sensor tips, to which the biomolecules of interest are coupled. The sensor tips are then immersed in a solution containing a potential binding partner. When these molecules interact, they bind to the sensor, creating a change in the thickness of the biolayer on the sensor tip. This shift alters the interference pattern of white light reflected from the sensor surface, which is directly measured and translated into real-time kinetic data.
The BLI technique does not require any microfluidics or sample flow. Instead, an orbital flow is created by shaking the microwell-plates that contain the samples and into which the optical sensors are dipped. Therefore, BLI works great with complex, viscous bioliquids like serum or cell lysate.
Deduced Parameters
kon (ka) - Association rate constant. Provides information on how fast complexes form; can be used for KD determination.
koff (kd) - Dissociation rate constant. Provides information on how fast complexes dissociate; can be used for KD determination.
KD - Equilibrium dissociation constant. Can be obtained by kinetic or classical equilibrium binding analysis. Provides information about the strength but not the dynamics of an interaction.
ΔH - Binding enthalpy. KD values at different temperatures can be used to obtain the binding enthalpy of an interaction via van't-Hoff-plots.
c - Molar concentration of biolgics (e.g. proteins, antibodies, antibody fragments) in supernatants, production mixtures, or crude lysates
Epitope specificity - High throughput epitope binning/cross competition assays for determining presence of distinct epitopes and selection of antibodies in drug discovery.
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