The need for new and potent antibiotics in an era of increasing multidrug resistance in bacteria has driven the search for new antimicrobial agents, including the design of synthetic antimicrobial peptides (AMPs). While a number of β-sheet forming AMPs have been proposed, their similarity to β-amyloids raises a number of concerns associated with neurodegenerative states. GL13K is an effective, synthetic AMP that selectively folds into β-sheets at anionic interfaces. Moreover, it is one of relatively few AMPs that preferentially fold into β-sheets without bridging disulfides. The interfacial activity of GL13K and its propensity to form amyloid fibrils have not been investigated. Using structural studies at the air/water interface and in the absence of anionic lipids, we demonstrate that while GL13K does form crystalline β-sheets, it does not self-assemble into fibrils. This work emphasizes the requirement for a single charged amino acid in the hydrophobic face to prevent fibril formation in synthetic peptides.

中文翻译：

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抗菌肽GL13K到非原纤维结晶β-Sheets的界面自组装。

在细菌对多药耐药性不断提高的时代，对新型强效抗生素的需求推动了对新抗菌剂的探索，包括合成抗菌肽（AMPs）的设计。尽管已经提出了许多形成β-折叠的AMP，但是它们与β-淀粉样蛋白的相似性引起了许多与神经退行性状态有关的担忧。GL13K是一种有效的合成AMP，可在阴离子界面选择性折叠成β-折叠。而且，它是相对较少的AMP之一，可优先折叠成β-折叠而不会桥接二硫键。尚未研究GL13K的界面活性及其形成淀粉样蛋白原纤维的倾向。通过在空气/水界面处和没有阴离子脂质的情况下进行结构研究，我们证明了GL13K确实形成了结晶β-折叠，它不会自组装成原纤维。这项工作强调在疏水面上需要一个带电荷的氨基酸，以防止合成肽中的原纤维形成。