Nanoribbons self-assembled from short peptides demonstrate the formation of polar zippers between β-sheets.

ABSTRACT: Peptide self-assembly is a hierarchical process, often starting with the formation of α-helices, β-sheets or β-hairpins. However, how the secondary structures undergo further assembly to form higher-order architectures remains largely unexplored. The polar zipper originally proposed by Perutz is formed between neighboring β-strands of poly-glutamine via their side-chain hydrogen bonding and helps to stabilize the sheet. By rational design of short amphiphilic peptides and their self-assembly, here we demonstrate the formation of polar zippers between neighboring β-sheets rather than between β-strands within a sheet, which in turn intermesh the β-sheets into wide and flat ribbons. Such a super-secondary structural template based on well-defined hydrogen bonds could offer an agile route for

SUBMITTER: Wang M 

PROVIDER: S-EPMC6269506 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature