Aromatic-Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels.
Aromatic-Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels.
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DOI：
10.1021/jacs.6b11512
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发表时间：
2017-01-11
影响因子：
15
通讯作者：
Xu B
中科院分区：
文献类型：
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作者：
Li J;Du X;Hashim S;Shy A;Xu B
由于缺乏蛋白质的限制，分离的短肽通常无法维持其原始的二级结构。在这里，我们展示了来自蛋白质 β-折叠基序的两个互补五肽，在其 C 端连接到芳香基序（即芘），在混合时自组装形成 β-折叠状结构。除了使自组装能够在混合时产生超分子水凝胶之外，芳香族-芳香族相互作用还促进五肽从α-螺旋构象转变为β-折叠构象。作为利用芳香族-芳香族相互作用来模拟蛋白质构象限制的第一个例子，这项工作展示了一种生物启发的方法，通过使用蛋白质结构作为蓝图的合理设计来生成具有预定义的肽二级结构的肽纳米纤维。
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.