Design of Multicomponent Peptide Fibrils with Ordered and Programmable Compositional Patterns

Abstract

Advanced applications of biomacromolecular assemblies require a stringent degree of control over molecular arrangement, which is a challenge to current synthetic methods. Here we used a neighbor-controlled patterning strategy to build multicomponent peptide fibrils with an unprecedented capacity to manipulate local composition and peptide positions. Eight peptides were designed to have regulable nearest neighbors upon co-assembly, which, by simulation, afforded 412 different patterns within fibrils, with varied compositions and/ or peptide positions. The fibrils with six prescribed patterns were experimentally constructed with high accuracy. The controlled patterning also applies to functionalities appended to the peptides, as exemplified by arranging carbohydrate ligands at nanoscale precision for protein recognition. This study offers a route to molecular editing of inner structures of peptide assemblies, prefiguring the uniqueness and richness of patterning-based material design.

A matter of charge: Electrostatically tuned coassembly of amphiphilic peptides

“…β-sheet peptides were found to coassemble with blood-clotting proteins in a manner that may be relevant to coagulation 38 . Coassemblies of peptide mixtures (PM) were explored with collagen-like short motifs 39,40 , -helical 41 , and chiral dependent β-sheet structures [42][43][44] . These PM coassemblies exhibited various morphologies, like flat and twisted ribbons, sheets and fibrils 31,32 .…”