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首页> 外文期刊>Chemistry: A European journal >Self-Assembly of Amylin(20-29)Amide-Bond Derivatives into Helical Ribbons and Peptide Nanotubes rather than Fibrils
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Self-Assembly of Amylin(20-29)Amide-Bond Derivatives into Helical Ribbons and Peptide Nanotubes rather than Fibrils

机译：Amylin（20-29）酰胺键衍生物的自组装成螺旋带和肽纳米管而不是原纤维

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Uncontrolled aggregation of proteins or polypeptides can be detrimental for normal cellular processes in healthy organisms.Proteins or polypeptides that form these amyloid deposits differ in their primary sequence but share a common structural motif:the(anti)parallel beta sheet.A well-accepted approach for interfering with beta-sheet formation is the design of soluble 13-sheet peptides to disrupt the hydrogen-bonding network;this ultimately leads to the disassembly of the aggregates or fibrils.Here,we describe the synthesis,spectroscopic analysis,and aggregation behavior,imaged by electron microscopy,of several backbone-modified amylin(20-29)derivatives.It was found that these amylin derivatives were not able to form fibrils and to some extent were able to inhibit fibril growth of native amylin(20-29).However,two of the amylin peptides were able to form large supramolecular assemblies,like helical ribbons and peptide nanotubes,in which beta-sheet formation was clearly absent.This was quite unexpected since these peptides have been designed as soluble beta-sheet breakers for disrupting the characteristic hydrogen-bonding network of(anti)parallel beta sheets.The increased hydrophobicity and the presence of essential amino acid side chains in the newly designed amylin(20-29)derivatives were found to be the driving force for self-assembly into helical ribbons and peptide nanotubes.This example of controlled and desired peptide aggregation may be a strong impetus for research on bionanomaterials in which special shapes and assemblies are the focus of interest.
机译：蛋白质或多肽的不受控制的聚集对于健康生物体的正常细胞过程可能是有害的。形成这些淀粉样蛋白沉积物的蛋白质或多肽的主要序列不同，但具有共同的结构基序:(反）平行β折叠。干扰β-折叠形成的方法是设计可溶的13-折叠肽来破坏氢键网络;这最终导致聚集体或原纤维的分解。在此，我们描述了合成，光谱分析和聚集行为，用电子显微镜对几种主链修饰的胰岛淀粉样多肽（20-29）衍生物进行成像。发现这些胰岛淀粉样多肽衍生物不能形成原纤维，并且在一定程度上能够抑制天然胰岛淀粉样多肽（20-29）的生长。但是，两种胰岛淀粉样多肽肽能够形成大的超分子组装体，例如螺旋带和肽纳米管，其中显然没有β-折叠的形成。出乎意料的是，这些肽已被设计为可溶的β-折叠阻滞剂，用于破坏（反）平行β折叠的特征性氢键网络。疏水性的增加和新设计的胰岛淀粉样多肽中必需氨基酸侧链的存在（20- 29）发现衍生物是自组装成螺旋带和肽纳米管的驱动力。这个受控和理想的肽聚集的例子可能是研究以特殊形状和组装为关注焦点的生物纳米材料的强大动力。

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