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Interaction Analysis

Interaction analysis by biophysical methods provides detailed insights into exactly how potential drug candidates bind to their target biomolecules and facilitates the identification of novel drug candidates with improved efficacy and selectivity. We employ a wide range of techniques including surface plasmon resonance (SPR), grating-coupled interferometry (GCI), isothermal titration calorimetry (ITC), differential scanning fluorimetry (DSF), nuclear magnetic resonance (NMR), and X-ray crystallography to fully interrogate the interaction. These methods utilize physical principles to study not only the binding affinity but also important parameters such as thermodynamics, kinetics, stoichiometry and structural aspects of drug-target interactions.

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A more in-depth view

Example

SPR and GCI allows real-time monitoring of binding events, enabling the determination of association and dissociation rates, equilibrium constants, and specificity of interactions. ITC measures the heat released or absorbed during a binding event, providing thermodynamic information crucial for understanding the energetics of drug binding. NMR and X-ray crystallography, on the other hand, offer high-resolution structural details of the drug-target complex, aiding in the rational design and optimisation of drug candidates. By characterising parameters such as the binding kinetics and thermodynamics, we can prioritise lead compounds based on their interaction profiles. Additionally, the structural information obtained from techniques like NMR and X-ray crystallography allows us to rationally modify the drug structures to fine-tune their interactions with target proteins, minimizing off-target effects and improving safety profiles.

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