肽和蛋白纳米材料：设计的挑战

关键词： 蛋白质，肽，纳米材料
出版时间: 2015-11-10
在纳米尺寸上通过结构定义纳米材料在合理设计，最困难的是造结构分析上一直以来都迎来了巨大的挑战。特定序列的生物分子、蛋白和核酸在构建这些类型的纳米材料都有些许优势，因为序列和高有序的结构能够得到它们之间相关关系，从而能够通多在连续结构层次上进行分子水平上编码以控制具有有序功能特性的纳米材料。然而，在预测自组装结构的设计中需在肽亚基之间界面的精确控制。相对于蛋白的三级结构，四级结构在蛋白与蛋白界面之间的残基突变推测是不稳定的。研究人员通过使用简单自组装的肽系统以在纳米管和纳米片之间的界面上解释设计的合理性。
因此，这些肽系统提供了一个框架，以了解在演化中小肽序列怎么能在超分子结构中转化为非常大的改变，以提供较明显的证据（蛋白界面之间的可设计性在自组装系统控制超分子结构中要重点考虑。）

Structurally defined materials on the nanometer length-scale have been historically the most challenging to rationally construct and the most difficult to structurally analyze. Sequence-specific biomolecules, proteins and nucleic acids, have advantages as design elements for construction of these types of nano-scale materials in that correlations can be drawn between sequence and higher order structure, potentially affording ordered assemblies in which functional properties can be controlled through the progression of structural hierarchy encoded at the molecular level. However, the predictable design of self-assembled structures requires precise structural control of the interfaces between peptide subunits (protomers). In contrast to the robustness of protein tertiary structure, quaternary structure has been postulated to be labile with respect to mutagenesis of residues located at the protein-protein interface. The researchers have employed simple self-assembling peptide systems to interrogate the concept of designability of interfaces within the structural context of nanotubes and nanosheets. 

Thus, these peptide systems provide a framework for understanding how minor sequence changes in evolution can translate into very large changes in supramolecular structure, which provides significant evidence that the designability of protein interfaces is a critical consideration for control of supramolecular structure in self-assembling systems.

参考文献：Peptide and protein nanomaterials: the design challengeb