| Summary: | Over the last decade self-assembling peptide systems have attracted considerable interest as novel biomaterials for use in different applications including tissue regeneration and cosmetics. Peptide-based biomaterials are assembled from small building blocks from the bottom up. This study is focused on the use of different peptide folding motifs as building blocks for the construction of fibrous biomaterials. Different peptide amphiphiles (PAs) were synthesized using solid phase synthesis and their folding, self-assembly and biological properties were characterized using circular dichroism (CD) spectroscopy, transmission electron microscopy (TEM) and minimal inhibitory concentration (MIC) assays. CD spectra showed random coil and β-sheet conformations for the amphiphiles. TEM revealed nanoscale fibre structures for most of the PA’s, some of which displayed antimicrobial activity. Effectively, the results demonstrate that the designed peptide self-assembles into nanofibre suprastructures. However, the peptides were not strongly antimicrobial and formed fibrillar structures. This work introduces new biomaterial designs with potential applications as nanofibre scaffolds for tissue engineering.
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