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N-N atropisomers represent a useful class of compounds that has recently received important attention from many research groups. This article presents an in-depth analysis of the energy barrier needed for the racemization process of atropoisomeric hydrazides, combining an experimental and computational approach. The focus is on examining how electronic and steric factors impact the racemization process. The results obtained indicate that the barrier observed during the racemization process mainly arises from an increase in the p-orbital character of the nitrogen atoms.

S-nitrosothiols (RSNOs) are a group of sulfur-containing compounds biologically involved in nitric oxide (NO˙) release and signalling pathway. NO˙ plays important physiological and pharmacological activities, particularly in vasodilation and in inducing muscle relaxation. Several RSNO compounds have been detected in biological systems, and many of them have been chemically synthesized in the laboratory. To date, no works describing the synthesis of the S-nitrosopantetheine (SNOPANT) are reported in the literature. Taking into account that pantetheine is a biological thiol with a crucial function in metabolism, its nitrosylation in vivo could play a role in various metabolic signalling pathways. In this paper, the synthesis and the chromatographic determination of SNOPANT is reported for the first time, as well as a brief investigation of its reactivity in aqueous solutions in the presence of factors known to affect its stability.

In High-Performance Liquid Chromatography (HPLC), the separation of reducing sugars can typically show three possible typologies of chromatographic profiles (i.e., single peak, two resolved peaks and two peaks interconnected by a plateau) due to the rate at which the relevant α/β anomers interconversion (anomerization) can take place in relation to their elution-time. By analyzing these chromatographic profiles, thermodynamic and kinetic properties of anomerization phenomenon can be extrapolated. In this work we studied the anomerization of some monosaccharides by using a recently developed photo-click cysteine-based stationary phase through dynamic hydrophilic interaction liquid chromatography (D-HILIC) conditions. In the 5–25 °C temperature range, the ΔG#α→β and ΔG#β→α barriers were found to achieve values within the interval 21.1/22.2 kcal/mol for glucose, with differences between α→β and β→α reactions of about 0.4 kcal/mol. For xylose, in the same temperature range, the ΔG#α→β and ΔG#β→α barriers are between 20.7 to 21.5 kcal/mol, with differences between α→β and β→α reactions of about 0.2 kcal/mol. The experimental data are in agreement with those reported in literature, confirming the this new stationary phase using HILIC conditions is a robust platform to measure kinetic and thermodynamic properties of the isomerization reaction.

Bioactive peptides are increasingly used in clinical practice. Reversed-phase chromatography using formic or trifluoroacetic acid in the mobile phase is the most widely used technique for their analytical control. However, sometimes it does not prove sufficient to solve challenging chromatographic problems. In the search for alternative elution modes, the dynamic electrostatic repulsion reversed-phase was evaluated to separate eight probe peptides characterised by different molecular weights and isoelectric points. This technique, which involves TBAHSO4 in the mobile phase, provided the lowest asymmetry and peak width at half height values and the highest in peak capacity (about 200 for a gradient of 30 min) and resolution concerning the classic reversed-phase. All analyses were performed using cutting-edge columns developed for peptide separation, and the comparison of the chromatograms obtained shows how the dynamic electrostatic repulsion reversed-phase is an attractive alternative to the classic reversed-phase.