Ligand Binding Studies
and Binder Affinities

Our ligand binding capabilities leverage both ligand-observed and target-observed NMR methods, enabling the identification of small-molecule binders, as well as protein–protein, nucleic acid, and peptide–target interactions. A key advantage of NMR-based ligand binding studies is that experiments are performed under physiologically relevant conditions, ensuring results that closely reflect true biological behavior.
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Ligand-Observe Methods (e.g. STD/ waterLOGSY/ CPMG)
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​These experiments focus on the spectral properties of the ligand, are not limited by target size and can provide the following information:
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Provide rapid turnaround with high sensitivity
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Require only small amounts of target and compound
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Deliver a clear yes/no assessment of ligand binding
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Offer insights into the nature of ligand–target interactions
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Determine ligand binding stoichiometry
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Target Observe Methods (e.g. HSQC/HMQC)​​​​
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These experiments focus on the spectral properties of the target and provide powerful insights into:
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Provide powerful insights into ligand binding site location
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Reveal conformational changes in the target upon ligand binding
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Deliver mechanistic understanding that can serve as a cornerstone for the chemistry/biology in therapeutic programs
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Typically require 2D NMR methods and an isotopically labeled target
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Binding constant determination (Kd)
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Both ligand and target observe experiments can be used to accurately and precisely measure the affinity (dissociation constant, Kd) of ligands to their targets under biologically relevant conditions.
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