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- W3153698892 abstract "Controlling the spatial and temporal behavior of peptide segments is essential in the fabrication of functional peptide-based materials and nanostructures. To achieve a desired structure, complex sequence design is often required, coupled with the inclusion of unnatural amino acids or synthetic modifications. Herein, we investigate the structural properties of 1:1 inclusion complexes between specific oligopeptides and cucurbit[8]uril (CB[8]), inducing the formation of turns, and by alteration of the peptide sequence, tunable structural chirality. We also explore extended peptide sequence binding with CB[8], demonstrating a simple approach to construct a peptide hairpin." @default.
- W3153698892 created "2021-04-26" @default.
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- W3153698892 date "2021-04-16" @default.
- W3153698892 modified "2023-10-18" @default.
- W3153698892 title "Host–Guest Induced Peptide Folding with Sequence-Specific Structural Chirality" @default.
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- W3153698892 doi "https://doi.org/10.1021/jacs.1c00342" @default.
- W3153698892 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8154536" @default.
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