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This study presents for the first time the polymerization of methyl methacrylate (MMA) in the presence of poly(vinyl chloride) (PVC) that takes place by both SARA-ATRP and SET-LRP mechanisms. The two types of polymerizations that occur in the system are PMMA grafting to the PVC backbone and the formation of a new PMMA polymer, both occurring in the presence of a Cu 0 wire. The polymerizations were controlled as confirmed by the molecular weight evolution, polymerization kinetics, and variations in the dispersity value. The MMA polymerization in the presence of PVC at 60 and 70 °C leads to the formation of two polymer species characterized by an increase in the molecular weight with the conversion and a narrowing of the dispersity value with the reaction progress. To increase the degree of control over the polymerization, the same reaction was performed at room temperature, which allowed us to highlight the presence of the SARA-ATRP and SET-LRP mechanisms via subsequent polymer chain extensions. The results demonstrated that PMMA grafting on PVC polymers follows a SARA-ATRP mechanism, while the formation of a PMMA homopolymer entails a SET-LRP process. The influence of solvent nature on the polymerization reaction was studied by performing the grafting of N -isopropylacrylamide (NIPAM) onto the surface of PVC particles in aqueous media in the presence and in the absence of CuCl 2 . The polymerization reactions and the obtained materials were studied by gel permeation chromatography (GPC), 1 H NMR, DMA, scanning electron microscopy (SEM), and atomic force microscopy (AFM)., Competing Interests: The authors declare no competing financial interest., (© 2024 The Authors. Published by American Chemical Society.)

Protein and peptide interactions are characterized in the liquid state by multidimensional NMR spectroscopy experiments, which can take hours to record. We show that starting from hyperpolarized HDO, two-dimensional (2D) proton correlation maps of a peptide, either free in solution or interacting with liposomes, can be acquired in less than 60 s. In standard 2D NMR spectroscopy without hyperpolarization, the acquisition time required for similar spectral correlations is on the order of hours. This hyperpolarized experiment enables the identification of amino acids featuring solvent-interacting hydrogens and provides fast spectroscopic analysis of peptide conformers. Sensitivity-enhanced 2D proton correlation spectroscopy is a useful and straightforward tool for biochemistry and structural biology, as it does not recur to nitrogen-15 or carbon-13 isotope enrichment.