Academic Scientific JournalsResearch on the fibrilization, stability and antimicrobial activity of the new self-assembling antimicrobial peptides with short fibrillogenic sequences
DOI:
https://doi.org/10.26881/prog.2023.12.02Keywords:
peptide fibrils, self-assembly peptides, biomaterials, antimicrobial peptidesAbstract
The search for effective antimicrobial active substances is a very important and current topic, but at the same time, it remains a big problem for modern medicine. This is caused by bacterial resistance to antibiotics, tumor’s development and the lack of effective drugs for treatment. One possibility for a solution of these problems is that of peptides with antimicrobial activity (Antimicrobial peptides, AMPs). Their effectiveness is associated with the interaction between them and cell membranes. However, a significant challenge in their application is their relatively low stability. One of the methods that lead to increased stability is to combine bioactive peptides with scaffolds. An example of a scaffold is that of peptide fibrils, which are highly ordered structures that have a tendency to self-assembly, which ensures homogeneity and high stability. In addition, the scaffolds may be functionalized by different bioactive sequences. In our project, we connected fibrillogenic sequences, formed in a steric zipper, to antimicrobial sequences based on human cathelicidin (LL-37), which resulted in creation of new self-assembling antimicrobial peptides. We synthesized all peptides in the solid state using Fmoc-methodology. Many tests, such as to check the tendency to fibril formation as well as antimicrobial activity, were done. The conducted research allowed us to determine the potential of fibrillogenic sequences as carriers as well as their impact on antimicrobial activity.
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