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Ligand Binding Studies

and Binder Affinities

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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

  • Require only small amounts of target and compound

  • Deliver a clear yes/no assessment of ligand binding

  • Offer insights into the nature of ligand–target interactions

  • 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

  • Reveal conformational changes in the target upon ligand binding

  • Deliver mechanistic understanding that can serve as a cornerstone for the chemistry/biology in therapeutic programs

  • 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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1 Mifflin Place, Suite 400

Cambridge, MA 02138 

Tel. 978-496-0666

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