Engineering the Ionic Self-Assembly of Polyoxometalates and Facial-Like Peptides
Engineering the Ionic Self-Assembly of Polyoxometalates and Facial-Like Peptides
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多金属氧酸盐和面部样肽的离子自组装工程
DOI：
10.1002/chem.201602449
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发表时间：
2016-10-24
影响因子：
4.3
通讯作者：
Li, Wen
中科院分区：
文献类型：
--
作者：
Li, Jingfang;Li, Xiaodong;Li, Wen
系统地研究了多金属氧酸盐（PMs）和带有赖氨酸残基的类面阳离子肽的自组装行为。圆二色性和紫外/可见光谱表明，多阴离子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β-折叠状态的构象转变，并随后发生共组装。透射电子显微镜（TEM）和原子力显微镜（AFM）测量显示，随着PMs尺寸的减小或肽分子间作用力（如氢键、疏水作用和/或π - π相互作用）的增加，形成了均匀的纳米纤维。此外，通过合理抑制覆盖在纳米结构表面的壳肽的静电排斥，可以提高纳米结构的稳定性。这些结果为理解肽和PMs的离子自组装以及控制它们的最终形态提供了新的见解。
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.