Molecularly tuned peptide assemblies at the liquid-solid interface studied by scanning tunneling microscopy.

Molecularly tuned peptide assemblies at the liquid-solid interface studied by scanning tunneling microscopy.
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DOI:
10.1039/b923927h
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发表时间:
2010-09
期刊:
Physical chemistry chemical physics : PCCP
影响因子:
--
通讯作者:
Lin Niu;Xiaojing Ma;Lei Liu;Xiaobo Mao;Dongxia Wu;Yanlian Yang;Q. Zeng;Chen Wang
Lin Niu;Xiaojing Ma;Lei Liu;Xiaobo Mao;Dongxia Wu;Yanlian Yang;Q. Zeng;Chen Wang
中科院分区:
其他
文献类型:
--
作者:
Lin Niu;Xiaojing Ma;Lei Liu;Xiaobo Mao;Dongxia Wu;Yanlian Yang;Q. Zeng;Chen Wang

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在这里,我们报道了利用扫描隧道显微镜(STM)在液-固界面上用分子模板对多肽组件进行调制。观察到五肽5Ala的组装呈层状结构,三联吡啶衍生物(BT-O-C16)的引入导致了五肽单体和二聚体被包裹在BT-O-C16网络的纳米空腔中的共组装分子结构。分子网络的选择性使有机多肽结构的可编程构建成为可能。
We report here the modulation of a peptide assembly with a molecular template at the liquid-solid interface using scanning tunneling microscopy (STM). A lamella structure is observed for the assembly of pentapeptide 5Ala, and the introduction of the terpyridine derivative (BT-O-C16) gives rise to co-assembled molecular architectures with pentapeptide monomers and dimers encapsulated in the nanoscale cavities of the BT-O-C16 network. The selectivity of the molecular networks could allow for programmable construction of organic-peptide architectures.