Aromatic–Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels

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• 作者：Jie Li ; Xuewen Du ; Saqib Hashim ; Adrianna Shy ; Bing Xu
• 刊名：Journal of the American Chemical Society
• 出版年：2017
• 出版时间：January 11, 2017
• 年：2017
• 卷：139
• 期：1
• 页码：71-74
• 全文大小：375K
• ISSN：1520-5126

文摘

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.