A straightforward method for measuring binding affinities of ligands to proteins of unknown concentration in biological tissues

Abstract
The equilibrium dissociation constant (Kd) is a quantitative measure of the strength with which a drug binds to its receptor. Methods for determining Kd typically require a priori knowledge of protein concentration or mass. We report a simple dilution method for estimation of Kd using native mass spectrometry which can be applied to protein–ligand complexes involving proteins of unknown concentration, from complex mixtures, including direct tissue sampling.

Advion Interchim Scientific^® Triversa^® NanoMate^® (Advion, Ithaca, NY) was utilized.

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