Tuning One-Dimensional Nanostructures of Bola-Like Peptide Amphiphiles by Varying the Hydrophilic Amino Acids
Tuning One-Dimensional Nanostructures of Bola-Like Peptide Amphiphiles by Varying the Hydrophilic Amino Acids
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通过改变亲水性氨基酸来调节 Bola 样肽两亲物的一维纳米结构
DOI：
10.1002/chem.201601309
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
Lu Jian R.
中科院分区：
文献类型：
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作者：
Zhao Yurong;Deng Li;Yang Wei;Wang Dong;Pambou Elias;Lu Zhiming;Li Zongyi;Wang Jiqian;King Stephen;Rogers Sarah;Xu Hai;Lu Jian R.
通过实验测量和计算机模拟相结合，我们发现对于类bola肽两亲体XI4X，当X=K， R和H时，亲水性氨基酸取代对肽骨架之间β-片氢键的影响很小。然而，所有肽自组装成一维（1D）纳米结构，具有完全不同的形态，即KI4K的纳米管和螺旋纳米带，HI4H的纳米带是扁平的多层纳米带，RI4R的纳米带是扭曲的双层纳米带。这些不同的一维形态可以解释为三个肽β-片在x方向（宽度）和z方向（高度）上不同的堆叠程度和模式，微观上源于片与溶剂分子的氢键能力以及β-片单层之间亲水性氨基酸侧链通过堆叠相互作用和氢键的配对。这些不同的一维纳米结构具有不同的表面化学和功能，在开发这些亲水性氨基酸各自性质的各种应用中具有很大的潜力。
By combining experimental measurements and computer simulations, we here show that for the bola-like peptide amphiphiles XI4X, where X=K, R, and H, the hydrophilic amino acid substitutions have little effect on the β-sheet hydrogen-bonding between peptide backbones. Whereas all of the peptides self-assemble into one dimensional (1D) nanostructures with completely different morphologies, that is, nanotubes and helical nanoribbons for KI4K, flat and multilayered nanoribbons for HI4H, and twisted and bilayered nanoribbons for RI4R. These different 1D morphologies can be explained by the distinct stacking degrees and modes of the three peptide β-sheets along the x-direction (width) and the z-direction (height), which microscopically originate from the hydrogen-bonding ability of the sheets to solvent molecules and the pairing of hydrophilic amino acid side chains between β-sheet monolayers through stacking interactions and hydrogen bonding. These different 1D nanostructures have distinct surface chemistry and functions, with great potential in various applications exploiting the respective properties of these hydrophilic amino acids.