| Abstract: | In the focus of the summarized PhD thesis are proteinogenic amino acids, which in
spite of being the elementary building blocks of all living organisms, have not yet been
sufficiently examined in terms of their ability to self-organize, and this characteristic feature
was observed with all amino acids investigated within the framework of this study.
Spontaneous self-organization of amino acids is observed in the abiotic solutions thereof and
it results in the formation of peptides, which in turn can organize to the more complex
structures, i.e., to the peptide nano- and microstructures.
In the course of the chromatographic investigations (HPLC-ELSD, HPLC-DAD, and
TLC) of the selected monocomponent and binary amino acid systems dissolved in an abiotic
environment, their ability was demonstrated to spontaneously undergo chiral inversion and /
or peptidization. Identification of the peptidization products was carried out with use of liquid
chromatography coupled with mass spectrometry. The microscopic assessment has confirmed
that simple peptides formed in the course of self-organization of amino acids can further
organize to the nano- and micropeptide structures, and the dependences were established
between the molecular structures of the initial amino acids and the shapes of the resulting
peptide nanostructures. In order to find an additional confirmation that spontaneous chiral
inversion really takes place in the solutions of proteinogenic amino acids, the polarimetric
measurements were performed and in purpose to confirm the oscillating nature of the
investigated peptidization processes, the turbidimetric measurements were performed as well.
Finally, the results of the biuret test have proved the presence of peptides in the examined
amino acid solutions. In collaboration with Prof. I.R. Epstein, the theoretical model was
elaborated which describes formation of the peptide nano- and microstructures in the binary
systems of the proteinogenic amino acids and elucidates the mechanisms playing crucial role
in these processes.
The research performed in the framework of this dissertation provides a better insight
in the phenomena of the self-organization of amino acids and peptides, which might perhaps
influence further progress in the field of molecular biology toward eliminating such factors
which accelerate deposition of the morbid amyloid aggregates in living organisms. On the
other hand, better understanding of the mechanisms resulting in the formation of the peptide
nano- and microstructures can help elaborate novel technologies of their formation without
use of a catalysts. |