Abstract
One critical step in new drugs development is the investigation of the interactions between drug candidate and target protein. Nuclear Magnetic Resonance Spectroscopy (NMR) is a well-established technique for studding these interactions. Due to its availability and structural similarities to human albumin, bovine serum albumin (BSA) is widely accepted as a model for investigating the binding of small molecules to serum albumin. We report here on the evaluation of binding interactions between BSA and 18 metabolites using saturation transfer difference (STD) NMR experiments. Positive STD signals that indicate metabolite-protein interactions were obtained for leucine, pyruvic acid, valine, threonine, alanine, 4-aminohippuric acid and tryptophan.
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