Self-assembly of constrained cyclic peptides controlled by ring size

Abstract

The de novo design of new peptide assemblies that expands the repertoire of biomaterial nanostructures has been of a tremendous challenge. Hence, it is evident that a successful research achievement in this area would increase the understanding of molecular interactions in supramolecules and create novel scaffolds exploitable in biotechnology and synthetic biology. The manipulation of cyclic peptide self-assembly is particularly intriguing for this purpose. Herein, we report that a novel type of cyclic peptides, referred to as chiral tether constrained cyclic peptides (CCP), shows promising self-assembly properties. CCPs are the first example of a controllable assembly of all-L-α-cyclic peptides with different ring sizes. A noteworthy feature of the CCP system is good tolerance of different secondary structures, ring size, and peptide sequence. Based on this system, a variety of nanostructures could be constructed, which display different physical properties, rendering it an excellent platform for molecular interaction studies. Further, demonstrate potential applications of these peptide assemblies in bioimaging and energy storage.