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- W3080510188 abstract "Abstract The inherent ability of peptides to self‐assemble with directional and rationally predictable interactions has fostered a plethora of synthetic two‐dimensional (2D) supramolecular biomaterials. However, the design of peptides with hierarchical assembly in different dimensions across mesoscopic lengths remains a challenging task. We here describe the structural exploration of a d / l ‐alternating cyclic octapeptide capable of assembling one‐dimensional (1D) nanotubes in water, which subsequently pack laterally to form giant 2D nanosheets up to 500 μm long with a constant 3.2 nm thickness. Specific amino acid mutations allowed the mapping of structure–assembly relationships that determine 2D self‐assembly. Nine peptide modifications were studied, revealing key features in the peptide sequence that nanosheets tolerated, while a total of three peptide variants included modifications that compromised their 2D arrangement. These lessons will serve as guide and inspiration for new 2D supramolecular peptide designs." @default.
- W3080510188 created "2020-09-01" @default.
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- W3080510188 date "2020-10-12" @default.
- W3080510188 modified "2023-10-18" @default.
- W3080510188 title "Sequence Decoding of 1D to 2D Self‐Assembling Cyclic Peptides" @default.
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- W3080510188 doi "https://doi.org/10.1002/chem.202003265" @default.
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