EXPLORING SMALL MOLECULE INTERACTIONS WITH MEMBRANE PROTEINS USING FIDA

Understanding the intricate interactions between small molecules and membrane proteins is
pivotal for deciphering their biological functions and facilitating the development of drugs
targeting integral membrane proteins. However, characterizing these interactions in vitro presents
a signifi cant challenge, primarily due to the subtle mass changes between the ligand-free and
bound states of membrane proteins. This proves an obstacle for methods relying on a change in
molecular mass for detection of complex formation such as surface plasmon resonance, biolayer
interferometry, mass photometry, analytical ultracentrifugation, and microscale thermophoresis.
To circumvent this, one can turn to thermodynamics and employ isothermal titration calorimetry.
However, this approach is marred by high sample consumption, exacerbating the diffi culty of
producing substantial quantities of stable, monodisperse membrane proteins.

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