ArticleJournal of the American Chemical Society2024
Rapid Protein-Ligand Affinity Determination by Photoinduced Hyperpolarized NMR.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Combining photo-CIDNP and long-lived spin states enables high-contrast detection of weak protein-ligand interactions.Physical chemistry chemical physics : PCCP · 2026Article
- Predictions of Steady-State Photo-CIDNP Enhancement by Machine Learning.Journal of the American Chemical Society · 2025Article
- Dynamic nuclear polarization and chemically induced hyperpolarization: Progress, mechanisms, and opportunities.Magnetic resonance letters · 2025Review
- Photo-CIDNP for quantification of micromolar analytes in urine.Communications chemistry · 2025Article
- Halogen-Bond-MediatedThe journal of physical chemistry letters · 2025Article
- Parahydrogen Polarization in Reverse Micelles and Application to Sensing of Protein-Ligand Binding.Journal of the American Chemical Society · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binding affinity determination of protein-ligand complexes is a cornerstone of drug design. State-of-the-art techniques are limited by lengthy and expensive processes. Building upon our recently introduced novel screening method utilizing photochemically induced dynamic nuclear polarization (photo-CIDNP) NMR, we provide the methodological framework to determine binding affinities within 5-15 min using 0.1 mg of protein. The accuracy of our method is demonstrated for the affinity constants of peptides binding to a PDZ domain and fragment ligands binding to the protein PIN1. The method can also be extended to measure the affinity of nonphoto-CIDNP-polarizable ligands in competition binding experiments. Finally, we demonstrate a strong correlation between the ligand-reduced signals in photo-CIDNP-based NMR fragment screening and the well-established saturation transfer difference (STD) NMR. Thus, our methodology measures protein-ligand affinities in the micro- to millimolar range in only a few minutes and informs on the binding epitope in a single-scan experiment, opening new avenues for early stage drug discovery approaches.
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Registered trials
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