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首页> 外文期刊>Chemistry: A European journal >Engineering the Ionic Self-Assembly of Polyoxometalates and Facial-Like Peptides
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Engineering the Ionic Self-Assembly of Polyoxometalates and Facial-Like Peptides

机译：工程化多金属氧酸盐和类似面部多肽的离子自组装

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摘要

The self-assembly behavior of polyoxometalates (PMs) and facial-like cationic peptides carrying lysine residues were systematically investigated. Circular dichroism and UV/Vis spectra demonstrated that the multivalent electrostatic attractions between polyanionic PMs and short peptides with protonated lysine residues initiated the conformational transition of peptide molecules from random-coil to -sheet state, and subsequently the co-assembly. TEM and atomic force microscopy (AFM) measurements showed that uniform nanofibers formed with decreasing size of the PMs or increasing the intermolecular forces of the peptides, such as through hydrogen-bonding, hydrophobic, and/or - interactions. Additionally, the stability of the nanostructures can be improved by rational suppression of the electrostatic repulsion of the shell peptides covering the surface of the nanostructures. These results provide new insight into understanding the ionic self-assembly of peptides and PMs and controlling their final morphology.
机译：系统研究了多金属氧酸盐（PMs）和带有赖氨酸残基的面部样阳离子肽的自组装行为。圆二色性和UV / Vis光谱表明，聚阴离子PMs和带有质子化赖氨酸残基的短肽之间的多价静电吸引引发了肽分子从无规卷曲到折叠状态的构象转变，并随后发生了共组装。 TEM和原子力显微镜（AFM）测量表明，随着纳米颗粒尺寸的减小或肽的分子间力的增加，例如通过氢键，疏水和/或-相互作用，形成了均匀的纳米纤维。另外，可以通过合理地抑制覆盖纳米结构表面的壳肽的静电排斥来提高纳米结构的稳定性。这些结果为了解肽和PM的离子自组装并控制其最终形态提供了新的见解。

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