In our earlier investigations, we have discovered that a-amino acids
dissolved in water or aqueous-organic solvents undergo spontaneous oscillatory
chiral inversion and oscillatory peptidization in parallel, and the dynamics of these
processes strongly depends on the chemical structure of a given amino acid,
physicochemical characteristics of a solvent used, ambient temperature, etc. The
aim of this study was to perform a preliminary reconnaissance on the possible
impact of D2O on the dynamics of spontaneous behavior of the selected test aamino
acids (L-Phe, L-His, L-Pro and L-Cys) stored at 25 ± 0.5 C for the period of
1 week. As the measuring techniques, turbidimetry in continuous registration mode
and mass spectrometry were employed. For the sake of comparison, the analogous
results were presented for the discussed a-amino acids dissolved in the aqueous
organic solvents and originally published elsewhere. Based on a comparison of the
turbidimetric fingerprints, the dynamics of the turbidity changes in heavy water
have proved rather moderate. Mass spectrometric results provided a confirmatory
evidence witnessing to rather negligible peptide yields in heavy water. Thus, turbidimetric
and mass spectrometric data have served as complementary proofs of a
considerable hampering of spontaneous peptidization of a-amino acids in D2O
