| 초록 |
Peptide self-assembled nanostructures based on diphenylalanine (FF) can have an ordered β-sheet secondary structure, which can lead to the formation of spheres, cylinders, and tubes due to strong interaction of phenyl groups between adjacent derivatives. It has been widely utilized in biomedical applications such as drug delivery and tissue regeneration due to its structural stability and biocompatibility. In this study, a tyrosine-mediated crosslink inspired by the resilin of the dragonfly, vinegar fly, and beetle was introduced in the short peptides to adopt its characteristic that photoredox can occur and affect antiparallel structure to form 1D nanostructure. In this context, protein-mimetic structural evolution was studied. The assembly behavior with photo-crosslinking was proved by in-situ LP-TEM. This result indicates that nature-protein motion should be studied due to their packing sensitivity and geometric constraints, providing insights in the development of novel materials. |
