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

ABSTRACT: Peptide self-assembly is a hierarchical process, often starting with the formation of ?-helices, ?-sheets or ?-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 ?-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 ?-sheets rather than between ?-strands within a sheet, which in turn intermesh the ?-sheets into wide and flat ribbons. Such a super-secondary structural template based on well-defined hydrogen bonds could offer an agile route for the construction of distinctive nanostructures and nanomaterials beyond ?-sheets.

SUBMITTER: Wang M 

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

REPOSITORIES: biostudies-literature

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

Wang Meng M   Wang Jiqian J   Zhou Peng P   Deng Jing J   Zhao Yurong Y   Sun Yawei Y   Yang Wei W   Wang Dong D   Li Zongyi Z   Hu Xuzhi X   King Stephen M SM   Rogers Sarah E SE   Cox Henry H   Waigh Thomas A TA   Yang Jun J   Lu Jian Ren JR   Xu Hai H  

Nature communications 20181130 1

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, he  ...[more]

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