(S)-2-Amino-2-methyldec-9-enoic acid

Nitrosation reactions span a diverse range of applications, from biochemistry to industrially important processes. This study examines nitrosation of aminothiones in acidic solutions and re-evaluates currently accepted diffusion limits and the true nature of the nitrosating agent for nitrous acid initiated reactions. Experimental measurements from stopped-flow UV/vis spectrophotometry afforded derivation of equilibrium constants and reaction enthalpies. Apparent Keq corresponds to 559-382 M(-2) for thioacetamide (TA, 15-25 °C) and 12600-5590 M(-2) for thiourea (TU, 15-35 °C), whereas the reaction enthalpies amount to -27.10 ± 0.05 kJ for TA and -29.30 ± 0.05 kJ for TU. Theoretical calculations via a thermochemical cycle agree well with reaction free energies from experiments, with errors of -2-4 kJ using solvation method SMD in conjunction with hybrid meta exchange-correlation functional M05-2X and high-accuracy multistep method CBS-QB3 for gas-phase calculations. The kinetic rates increase with acidity at activation energies of 54.9 (TA) and 66.1 kJ·mol(-1) (TU) for the same temperature range, confirming activation-controlled reactions. At pH 1 and below, the main decomposition pathway for the S-nitroso species leads to formation of nitric oxide.

We synthesized and carried out the conformational analysis of several hybrid dipeptides consisting of an α-amino acid attached to a quaternary glyco-β-amino acid. In particular, we combined a S-glycosylated β(2,2)-amino acid and two different types of α-amino acid, namely, aliphatic (alanine) and aromatic (phenylalanine and tryptophan) in the sequence of hybrid α/β-dipeptides. The key step in the synthesis involved the ring-opening reaction of a chiral cyclic sulfamidate, inserted in the peptidic sequence, with a sulfur-containing nucleophile by using 1-thio-β-D-glucopyranose derivatives. This reaction of glycosylation occurred with inversion of configuration at the quaternary center. The conformational behavior in aqueous solution of the peptide backbone and the glycosidic linkage for all synthesized hybrid glycopeptides was analyzed by using a protocol that combined NMR experiments and molecular dynamics with time-averaged restraints (MD-tar). Interestingly, the presence of the sulfur heteroatom at the quaternary center of the β-amino acid induced θ torsional angles close to 180° (anti). Notably, this value changed to 60° (gauche) when the peptidic sequence displayed aromatic α-amino acids due to the presence of CH-π interactions between the phenyl or indole ring and the methyl groups of the β-amino acid unit.

Phosphorous-containing molecules are essential constituents of all living cells. While the phosphate functional group is very common in small molecule natural products, nucleic acids, and as chemical modification in protein and peptides, phosphorous can form P⁻N (phosphoramidate), P⁻S (phosphorothioate), and P⁻C (e.g., phosphonate and phosphinate) linkages. While rare, these moieties play critical roles in many processes and in all forms of life. In this review we thoroughly categorize P⁻N, P⁻S, and P⁻C natural organophosphorus compounds. Information on biological source, biological activity, and biosynthesis is included, if known. This review also summarizes the role of phosphorylation on unusual amino acids in proteins (N- and S-phosphorylation) and reviews the natural phosphorothioate (P⁻S) and phosphoramidate (P⁻N) modifications of DNA and nucleotides with an emphasis on their role in the metabolism of the cell. We challenge the commonly held notion that nonphosphate organophosphorus functional groups are an oddity of biochemistry, with no central role in the metabolism of the cell. We postulate that the extent of utilization of some phosphorus groups by life, especially those containing P⁻N bonds, is likely severely underestimated and has been largely overlooked, mainly due to the technological limitations in their detection and analysis.