The application of Saturation Transfer Difference (STD) NMR spectroscopy for the characterization of dispersant particle interactions is introduced. STD NMR has hitherto been applied, with great success, to the characterization of ligand-protein interactions and is currently a standard tool in biomolecular NMR spectroscopy. Nevertheless, the STD NMR technique has so far not yet crossed the boundaries of the biomolecular field. Here, we demonstrate that in spite of clear differences between a protein binding site and the surface of a pigment nanoparticle, the latter can also be subjected to STD NMR analysis, allowing us to detect (screen for) binding ligands, discriminate ligand from nonligand, and obtain information on the binding epitope. The approach should be generally applicable as long as the nanoparticle is comprised of a dense network of hydrogens, implicating almost all organic molecular nanocrystals. Thus it provides a novel investigative tool for the study of dispersions that is highly complementary to existing ones.

The information obtained about relevant reaction parameters can be greatly increased by monitoring concentration changes during a reaction. To achieve this goal, a fully automated system was designed which handles both sampling and analysis. The sampling system takes samples at predefined intervals, and also performs a number of tasks such as dilution, neutralization, filtration and analysis. The examples show the universal applicability of the device regarding to solvents, reaction media and reaction type. It is also demonstrated that the information, included in the concentration profiles, greatly increases our knowledge about the reaction. This increase in information, in conjunction with other data,for example calorimetry, could be used for reaction simulation software.