TruBind™ BSI System 100

IMG_6247_TruBind-with-Anastasia_RT_webConformation-Sensitive, Back-Scattering Interferometry

Back Scattering Interferometry (BSI) is a truly label-free optical measurement technique that senses conformation-based changes upon ligand binding to a target.

BSI is mass- and matrix-independent, enabling the technology to directly measure small molecule binding interactions with large, complex targets, integral membrane proteins, soluble protein targets and allosteric membrane and protein targets, all in native and native-like environments.

The TruBind BSI System 100 is the world’s first free solution, label-free biosensor that detects changes in molecular conformation that arise from molecular aggregation, molecular binding, or molecular solvatic (hydration) effects.

The TruBind BSI System 100 employs a simple optical train comprised of a coherent light source, a microfluidic interferometric channel and a CCD camera. The interaction of the laser with the sample fluid-filled channel results in a high-contrast interference fringe pattern. Fringe shift results from change in refractive index (RI) as molecular complexes form and alter target conformation. Assays employing discrete samples with constant target and titrated ligand concentrations allow compound affinity to be computed under equilibrium binding conditions.

CORE FUNCTIONALITY

•    Determine binding affinity for allosteric ligands
•    Characterize affinity- vs. efficacy-driven mechanism of action (MOA) for allosteric targets
•    Demonstrate target engagement of compounds where MOA is unclear by other means
•    Study target and ligand aggregation and aggregation inhibition
•    Affinity-rank compounds to understand SAR and guide medicinal chemistry
•    Secondary screening of hits from cell-based and in-vitro HTS assays
•    Complement phenotypic drug discovery through verification and quantification of target engagement

CORE FEATURES

•     Label-free, in-solution, tether-free assay format
•     Conformational change specificity
•     Complex matrix-tolerant
•     Mass-independent binding affinity
•     pM sensitivity
•     Low sample consumption
•     Rapid assay development

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