Determination of protein–ligand binding affinity by NMR: observations from serum albumin model systems
✍ Scribed by Lee Fielding; Samantha Rutherford; Dan Fletcher
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 165 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0749-1581
- DOI
- 10.1002/mrc.1574
No coin nor oath required. For personal study only.
✦ Synopsis
The usefulness of bovine serum albumin (BSA) as a model protein for testing NMR methods for the study of protein-ligand interactions is discussed. Isothermal titration calorimetry established the binding affinity and stoichiometry of the specific binding site for L-tryptophan, D-tryptophan, naproxen, ibuprofen, salicylic acid and warfarin. The binding affinities of the same ligands determined by NMR methods are universally weaker (larger KD). This is because the NMR methods are susceptible to interference from additional non-specific binding. The L-tryptophan-BSA and naproxen-BSA systems were the best behaved model systems.