FUNKCJONALNE AMYLOIDY I NANOSTRUKTURY FOLDAMEROWE – POZYTYWNE ASPEKTY ZJAWISKA AGREGACJI PEPTYDÓW

Proteins and peptides exhibit a natural tendency to aggregate, which is considered a highly undesirable feature, as it leads to difficulties in dissolving samples and often prevents the use of these biomolecules, i.e., for therapeutic purposes. Moreover, insoluble protein fibers with a β-sheet structure, known as amyloids, have been associated with a group of diseases referred to as amyloidosis and may play a role in certain neurodegenerative disorders. However, non-pathological amyloids with well-defined physiological functions, known as functional amyloids, have also been identified. In various organisms, these amyloids serve specific roles, such as forming and stabilizing bacterial biofilms or regulating the cell cycle. Additionally, peptides can be used to construct nanostructures intended for a range of applications, including smart drug delivery systems. Particularly useful in this context appear to be foldamers, so peptides that adopt a well-defined and stable structure in solution. In my research, I focus on various aspects of peptide aggregation, and in this article, I present examples of how this phenomenon can be utilized.