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- W2562103780 abstract "Isolated short peptides usually are unable to maintain their original secondary structures due to the lack of the restriction from proteins. Here we show that two complementary pentapeptides from a β-sheet motif of a protein, being connected to an aromatic motif (i.e., pyrene) at their C-terminal, self-assemble to form β-sheet like structures upon mixing. Besides enabling the self-assembly to result in supramolecular hydrogels upon mixing, aromatic-aromatic interactions promote the pentapeptides transform from α-helix to β-sheet conformation. As the first example of using aromatic-aromatic interactions to mimic the conformational restriction in a protein, this work illustrates a bioinspired way to generate peptide nanofibers with predefined secondary structures of the peptides by a rational design using protein structures as the blueprint." @default.
- W2562103780 created "2017-01-06" @default.
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- W2562103780 date "2016-12-22" @default.
- W2562103780 modified "2023-09-29" @default.
- W2562103780 title "Aromatic–Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels" @default.
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- W2562103780 doi "https://doi.org/10.1021/jacs.6b11512" @default.
- W2562103780 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5477776" @default.
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- W2562103780 hasPublicationYear "2016" @default.
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