Investigation of spontaneous non-linear peptidization dynamics and mechanism with selected [alpha]-amino acid pairs

Abstract

The goal of this study was to provide experimental evidence on the dynamics and mechanism of spontaneous oscillatory peptidization in an abiotic system with three a-amino acid pairs (L-Met-L-Ser, L-His-L-Thr, and L-Cys-L-Phg), and to discuss these data in the context of an earlier established theoretical model. For each individual a-amino acid in a monocomponent and binary system, the dynamics of peptidization was traced with aid of the high performance liquid chromatograph with the evaporative light scattering detector. As an auxiliary technique, mass spectrometry (MS) was employed to scrutinize structures of the resulting peptides. With L-Met-L-Ser and L-His-L-Thr, the dynamics of one amino acid (L-Met and L-Thr, respectively) dominated over that of its counterpart. With LCys- L-Phg, no such predominance of the dynamics of one a-amino acid over that of its counterpart was observed. Mass spectrometric results confirmed the formation of heteropeptides with each investigated a-amino acid pair. With L-Met-L-Ser, L-His- L-Thr, and L-Cys-L-Phg, synchronization of the oscillatory behavior in the binary systems was observed, witnessing to mutual cross-catalysis of the two counterparts, assumed by case 4 of the theoretical model.