Protein-Ligand Interaction Analyses with Nuclear Magnetic Resonance Spectroscopy Enhanced by Dissolution Triplet Dynamic Nuclear Polarization.
The journal of physical chemistry letters(2023)
摘要
Solution-state nuclear magnetic resonance spectroscopy (NMR) is a powerful method for the analysis of intermolecular interactions within a biomolecular system. However, low sensitivity is one of the major obstacles of NMR. We improved the sensitivity of solution-state C NMR for the observation of intermolecular interactions between protein and ligand using hyperpolarized solution samples at room temperature. Eutectic crystals composed of C-salicylic acid and benzoic acid doped with pentacene were hyperpolarized by dynamic nuclear polarization using photoexcited triplet electrons, and a C nuclear polarization of 0.72 ± 0.07% was achieved after dissolution. The binding of human serum albumin and C-salicylate was observed with several hundred times sensitivity enhancement under mild conditions. The established C NMR was applied for pharmaceutical NMR experiments by observation of the partial return of the C chemical shift of salicylate by competitive binding with other non-isotope-labeled drugs.
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关键词
nuclear magnetic resonance spectroscopy,protein–ligand interaction analyses,magnetic resonance,polarization,dissolution
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