Residue-Level Determination of Small-Molecule–Protein Affinities by Hydrogen–Deuterium Exchange Mass Spectrometry
) at global, peptide, and single amino acid resolution by fitting uptake-concentration relationships under EX2 exchange and Langmuir binding assumptions. The ability to determine affinity constants in a spatially resolved manner combined with the automation available in HDX-MS sample handling and data analysis enables quantitative mapping of ligand-protein interactions and provides a scalable approach for structure-activity relationship studies in drug discovery.
Authors
- Luma G. Magalhães (ORCID: https://orcid.org/0000-0002-9233-1063)
- Joel McMillan (ORCID: https://orcid.org/0000-0002-1829-5308)
- Glenn R. Masson (ORCID: https://orcid.org/0000-0002-1386-4719)
- T.C. Eadsforth (ORCID: https://orcid.org/0000-0002-6000-093X)
- G. A. Stewart
- De Lin (ORCID: https://orcid.org/0000-0002-8262-4903)
- Vincent L. G. Postis (ORCID: https://orcid.org/0000-0001-9251-4567)
- Kieran Cartmill (ORCID: https://orcid.org/0000-0003-2456-6650)
Institutions
- University of Dundee (GB)
- Drug Discovery Laboratory (Norway) (NO)
Publication Details
- Journal
- Journal of the American Society for Mass Spectrometry
- Published
- 2026-03-31
- DOI
- https://doi.org/10.1021/jasms.6c00020
- Primary Topic
- Mass Spectrometry Techniques and Applications
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- University of Dundee
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council