The application of the hierarchical approach for the construction of foldameric peptide self-assembled nanostructures

In this paper, we show that a hierarchical approach for the construction of nanofibrils based on alpha,beta-peptide foldamers is a rational method for the design of novel self-assembled nanomaterials based on peptides. Incorporation of a trans-(1S,2S)-2-aminocyclopentanecarboxylic acid residue into the outer positions of the model coiled-coil peptide led to the formation of helical foldamers, which was determined by circular dichroism (CD) and vibrational spectroscopy. The oligomerization state of the obtained peptides in water was established by analytical ultracentrifugation (AUC). The thioflavin T assay and Congo red methods showed that the obtained alpha,beta-peptides possess a strong tendency to aggregate, leading to the formation of self-assembled nanostructures, which were assessed by microscopic techniques. The location of the beta-amino acid in the heptad repeat of the coiled-coil structure proved to have an influence on the secondary structure of the obtained peptides and on the morphology of the self-assembled nanostructures.

Automated summary

In this paper, a hierarchical approach for constructing nanofibrils based on alpha,beta-peptide foldamers is proposed as a rational method for designing novel self-assembled nanomaterials. The incorporation of a specific amino acid residue resulted in the formation of helical foldamers, which was confirmed by spectroscopic techniques. The obtained alpha,beta-peptides showed a strong tendency to aggregate and form self-assembled nanostructures, as revealed by assays and microscopy. The location of the beta-amino acid in the coiled-coil structure affected the secondary structure and morphology of the self-assembled nanostructures.