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Detalle de: Spatially Resolved STD-NMR Applied to the Study of Solute Transport in Biphasic Systems: Application to Protein-Ligand Interactions

Title Spatially Resolved STD-NMR Applied to the Study of Solute Transport in Biphasic Systems: Application to Protein-Ligand Interactions
Abstract

Fluid biphasic systems are one of the most interesting dynamic systems in chemistry and biochemistry. In nuclear magnetic resonance (NMR) spectroscopy, the study of the solute dynamics across fluid biphasic systems requires the introduction of dedicated NMR methods, due to their intrinsic heterogeneity. Diffusion and spatially resolved NMR techniques represent a useful approach for dealing with the study of solutes in biphasic systems and have been applied lately with success. Nevertheless, other potential applications of NMR spectroscopy for biphasic systems remain to be explored. In this proof-of-concept communication, we specifically aimed to investigate whether solute exchange between two immiscible phases can be followed by NMR experiments involving transfer of magnetization. To that aim, we have used spatially resolved saturation transfer difference NMR (SR-STD NMR) experiments to analyze solute exchange by transfer of saturation from one phase to the other in a biphasic system and have explored which are the underlying mechanisms leading to the transfer of magnetization between phases and the limits of the approach. We hereby demonstrate that SR-STD NMR is feasible and that it might be implemented in pharmacological screening for binders of biological receptors or in the study of chemical and biochemical reactions occurring at interfaces.

Apa Reference Nepravishta, R., Monaco, S., Muñoz-García, J.C., Khimyak, Y.Z. & Angulo, J. (2019). Spatially Resolved STD-NMR Applied to the Study of Solute Transport in Biphasic Systems: Application to Protein-Ligand Interactions. Natural Product Communications, 14(5). 10.1177/1934578x19849789
Doi 10.1177/1934578x19849789
Publication Date May 2019
Publication Type Article
Researcher Juan Carlos Muñoz García
Ontology Experimental structure determination, Molecular Interactions/Docking
Research Groups
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