Direct observation of photo-crosslinking diphenylalanine based peptides by in-situ nanoimaging

Abstract

Peptide self-assembled nanostructures based on diphenylalanine (FF) derivatives can have an orderly beta-sheet secondary structure due to strong interactions of phenyl groups between adjacent derivatives and form nanospheres, nanocylinders, and nanotubes. In addition, its are widely applied in fields such as drug delivery and tissue regeneration due to structural stability and biocompatibility. In this study, the introduction of tyrosine amino acids involved in protein synthesis and photooxidation-reduction reaction limits the alignment of strong antiparallel structures and suggests a self-assembly control strategy to enable nanovesicle formation. This process can be confirmed through the assembly transformation behavior that occurs along with the photopolymerization, and this will be explained through an in-situ liquid cell transmission electron microscope. This indicates that in a peptide-based material design strategy, geometric limitations play an important role in molecular self-assembly.