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- W4200171169 abstract "Although it is well-known proteins and their complexes are hierarchically organized and highly ordered structures, it remains a major challenge to replicate their hierarchical self-assembly process and to fabricate multihierarchical architectures with well-defined shapes and monodisperse characteristic sizes via peptide self-assembly. Here we describe an amphiphilic short peptide Ac-I3GGHK-NH2 that first preassembles into thin, left-handed β-sheet nanofibrils, followed by their ordered packing into right-handed nanotubes. The key intermediate morphology and structures featuring the hierarchical process are simultaneously demonstrated. Further mechanistic exploration with the variants Ac-I3GGGK-NH2, Ac-I3GGFK-NH2, and Ac-I3GGDHDK-NH2 reveals the vital role of multiple His-His side chain interactions between nanofibrils in mediating higher-order assembly and architectures. Altogether, our findings not only advance current understanding of hierarchical assembly of peptides and proteins but also afford a paradigm of how to take advantage of side chain interactions to construct higher-order assemblies with enhanced complexities." @default.
- W4200171169 created "2021-12-31" @default.
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- W4200171169 date "2021-12-06" @default.
- W4200171169 modified "2023-10-17" @default.
- W4200171169 title "Ordered Packing of β-Sheet Nanofibrils into Nanotubes: Multi-hierarchical Assembly of Designed Short Peptides" @default.
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- W4200171169 doi "https://doi.org/10.1021/acs.nanolett.1c02944" @default.
- W4200171169 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34870987" @default.
- W4200171169 hasPublicationYear "2021" @default.
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