Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles.
Small amphipathic peptides are responsible for the assembly of cruciferin nanoparticles.
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DOI：
10.1038/s41598-017-07908-z
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发表时间：
2017-08-10
影响因子：
4.6
通讯作者：
Wu J
中科院分区：
文献类型：
--
作者：
Hong H;Akbari A;Wu J
两亲性肽是用于制造有序纳米结构的通用构建模块，由于其巨大的设计可能性和生物功能而受到广泛关注。然而，使用天然蛋白质中的两亲性肽来创建可调节的纳米结构具有挑战性，因为它们的异质性和形成聚集体的巨大倾向。在这里，我们通过整合自上而下和自下而上的方法，用十字花科素两亲性肽制造了两种明确的纳米颗粒。引入碱水解（pH 12，120°C，30 分钟）将完整的十字花科素分解成肽（自上而下）。然后在钙离子存在下将十字花科素肽及其组分组装成纳米颗粒（自下而上）。来自 10 kDa 截止膜的渗透物级分形成比未分级的十字花科素肽（CRU-NP，约 185 nm）更小的纳米颗粒（F1-NP）（约 82 nm）；静电和疏水相互作用是颗粒形成的主要驱动力。 LC-MS/MS 分析表明，小两亲肽（Xn1Zn2Xn3Zn4，n1–4 = 0~5）由交替的疏水性 (X) 和亲水性 (Z) 氨基酸组成，F1-NP 和 CRU-NP 的长度分别为 5-15 和 5-20 个残基，负责颗粒的形成。我们的研究确立了冷凝胶颗粒形成的机制是通过两亲性肽的组装。
Amphipathic peptides are versatile building blocks for fabricating well-ordered nanostructures, which have gained much attention owing to their enormous design possibilities and bio-functionalities. However, using amphipathic peptides from natural proteins to create tunable nanostructures is challenging because of their heterogeneity and great tendency to form aggregates. Here we fabricated two well-defined nanoparticles from cruciferin amphipathic peptides by integrating top-down and bottom-up approach. Alkali hydrolysis (pH 12, 120 °C for 30 min) was introduced to break down intact cruciferin into peptides (top–down). The cruciferin peptides and their fractions were then assembled into nanoparticles (bottom–up) in the presence of calcium ions. The permeate fraction from 10 kDa cut-off membrane formed smaller nanoparticles (F1-NPs) (around 82 nm) than that of unfractionated cruciferin peptides (CRU-NPs, around 185 nm); the electrostatic and hydrophobic interactions were the main driving forces for particle formation. LC-MS/MS analysis characterised that the small amphipathic peptides (Xn1Zn2Xn3Zn4, n1–4 = 0~5), composed of alternating hydrophobic (X) and hydrophilic (Z) amino acid with a length of 5–15 and 5–20 residues for F1-NPs and CRU-NPs, respectively, were responsible for particle formation. Our study established the mechanism of particle formation of the cold gelation is through assembly of amphipathic peptides.
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影响因子：
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作者：
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10.1073/pnas.0701980104
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