Use of dissolved hyperpolarized species in NMR: Practical considerations.

Hyperpolarization techniques that can transiently boost nuclear spin polarization are generally carried out at low temperature - as in the case of dynamic nuclear polarization - or at high temperature in the gaseous state - as in the case of optically pumped noble gases. This review aims at describing the various issues and challenges that have been encountered during dissolution of hyperpolarized species, and solutions to these problems that have been or are currently proposed in the literature. During the transport of molecules from the polarizer to the NMR detection region, and when the hyperpolarized species or a precursor of hyperpolarization (e.

Inductive Coupling and Flow for Increased NMR Sensitivity.

A device is proposed to enhance the NMR sensitivity of slowly relaxing nuclei, taking advantage of a controlled solution flow within a microfluidic circuit and microsized NMR detection. Unlike our previous work ( Carret et al. Anal.

Enhancing NMR of Nonrelaxing Species Using a Controlled Flow Motion and a Miniaturized Circuit.

In this article we show that circulation of the sample in a closed-loop circuit combined to microsized detection can lead to a significant signal NMR enhancement. We present an optimized NMR device based on a mini bubble-pump associated with fluidics and microdetection that can be installed on a commercial NMR spectrometer. In addition to a significant signal enhancement for slowly relaxing nuclei, we show that it enables more precise and frequent monitoring of chemical reactions.

The presence of an air-water interface affects formation and elongation of α-Synuclein fibrils.

The aggregation of human α-Synuclein (α-Syn) into amyloid fibrils is related to the onset of multiple diseases termed synucleinopathies. Substantial evidence suggests that hydrophobic-hydrophilic interfaces promote the aggregation of amyloidogenic proteins and peptides in vitro. In this work the effect of the air-water interface (AWI) on α-Syn aggregation is investigated by means of thioflavin T binding measurements, dynamic light scattering, size-exclusion chromatography, electron microscopy, and atomic force microscopy.