ArticleJournal of medicinal chemistry2026
High-Resolution Relaxometry for Fragment Screening.
Article in Journal of medicinal chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Characterizing weak molecular interactions remains a major challenge in drug discovery. Here, we demonstrate the power of high-resolution relaxometry (HRR), using a fast sample shuttle system, as a highly sensitive ligand-based screening method. By measuring longitudinal relaxation rates over a wide magnetic field range (2-600 MHz), we obtained site-specific Nuclear Magnetic Resonance Dispersion (NMRD) profiles for three ligands interacting with the catalytic domain of Human Matrix Metalloproteinase-12 (MMP-12). HRR unambiguously detects weak binding (KD ≈ 10-6-10-4) at protein concentrations as low as 2 μM. The analysis of the NMRD profiles provides direct, quantitative assessment of the complex dynamics, yielding a rotational correlation time in excellent agreement with the protein hydrodynamic properties. This enables discrimination between genuine protein-ligand binding and alternative processes like ligand aggregation, often observed in pan-assay interference compounds (PAINS). HRR therefore provides a robust, low-sample-consumption, physicochemical approach for fragment screening and characterization of protein-ligand complex dynamics.
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