Yan, B; Bunch, J (2025) A straightforward method for measuring binding affinities of ligands to proteins of unknown concentration in biological tissues. Chemical Science, 16 (20). pp. 8673-8681. ISSN 2041-6520

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Abstract

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

Item Type:	Article
Keywords:	protein, ligand binding, binding affinity, mass spectrometry, biological sample
Subjects:	Biotechnology > Biopharmaceutical Manufacturing and Characterisation
Divisions:	Chemical & Biological Sciences
Identification number/DOI:	10.1039/D5SC02460A
Last Modified:	11 Feb 2026 15:38
URI:	https://eprintspublications.npl.co.uk/id/eprint/10269