Interaction Analysis

Interaction analyses provide a window into the molecular mechanisms that drive therapeutic efficacy by determining the key parameters of an interaction: affinity, kinetics, stoichiometry, and thermodynamics. At Concept Life Sciences, we offer a comprehensive suite of biophysical methods for interaction analyses, characterising numerous types of biomolecular interactions. We are particularly skilled at analysing complex binding between various modalities such as antibodies, ADCs, PROTACS, molecular glues, membrane proteins, nucleic acids, LNPs, peptides and small molecules.

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 to fully interrogate the interaction:

Surface Plasmon Resonance (SPR)
Isothermal Titration Calorimetry (ITC)
Grating-Coupled Interferometry (GCI)
Thermal Shift/Differential Scanning Fluorimetry (DSF)
Microscale Thermophoresis (MST)
Nuclear Magnetic Resonance (NMR)
X-ray crystallography

These methods utilise 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. 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, minimising off-target effects and improving safety profiles.

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