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Self‐assembly of a Sequence‐shuffled Short Peptide Amphiphile Triggered by Metal Ions into Terraced Nanodome‐like Structures
Chemistry - An Asian Journal ( IF 4.1 ) Pub Date : 2020-01-29 , DOI: 10.1002/asia.201901715
Ramesh Singh 1 , Narendra Kumar Mishra 2, 3 , Puneet Gupta 4 , Khashti Ballabh Joshi 1
Affiliation  

We highlight the structural diversity of strategically designed two short peptide amphiphiles (sPAs) and describe their structure–function relationship studies. The shuffling of two key amino acids, that is, tyrosine and phenylalanine, in a designed sPA lead to a pair of constitutional isomers. Such small and strategic alteration can bring a substantial change in the self‐assembling pattern. Inspired from the naturally occurring metallopeptides, bioactive transition‐metal ions were used for constructing the unusual nanostructures. Use of appropriate metal ions created bigger differences between the properties of these isomers and hence the self‐assembly. Coordination of appropriate transition metal ions modifies the internal nanoscale structures of sPA, thus leading to the formation of vertically stacked terraced layers with decreasing size, which possess a high degree of dimensional regularity. We propose that such metal‐induced terraced nanodome‐like hierarchical self‐assembly may have relevance for specific biotechnology applications.

中文翻译:

由金属离子触发的序列改组的短肽两亲物自组装为梯形纳米球状结构。

我们着重介绍了经过战略设计的两个短肽两亲物(sPAs)的结构多样性,并描述了它们的结构-功能关系研究。在设计的sPA中,两个关键氨基酸(即酪氨酸和苯丙氨酸)的改组导致一对结构异构体。这种微小的战略性改变可能会带来自我组装模式的重大变化。受天然金属肽的启发,生物活性过渡金属离子被用于构建异常的纳米结构。使用适当的金属离子会在这些异构体的性质之间产生更大的差异,从而在自组装之间产生更大的差异。适当的过渡金属离子的配位会修饰sPA的内部纳米级结构,从而导致尺寸减小的垂直堆叠梯形层的形成,具有高度的尺寸规则性。我们认为这种金属诱导的梯状纳米球状分层自组装可能与特定的生物技术应用有关。
更新日期:2020-01-29
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