General Method for Peptide Recognition in Water through Bioinspired Complementarity
General Method for Peptide Recognition in Water through Bioinspired Complementarity
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DOI：
10.1021/acs.chemmater.9b01613
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发表时间：
2019-07-09
影响因子：
8.6
通讯作者：
Zhao, Yan
中科院分区：
文献类型：
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作者：
Fa, Shixin;Zhao, Yan
尽管进行了几十年的研究，但识别多肽的一般方法一直难以捉摸。紧密相关的多肽之间的强结合和选择性是生物应用所必需的，但通过合成受体很难实现。在高度特异的蛋白质-蛋白质和蛋白质-配体相互作用的启发下，通过在交联胶束中进行多肽模板聚合，制备了蛋白质尺寸的水溶性印迹纳米颗粒。疏水和极性相互作用的结合为所选三肽提供了微摩尔到亚微摩尔的结合亲和力。鉴定出一对功能单体可增强结合的亲和力和选择性，并能够区分细微不同的序列，包括精氨酸对赖氨酸的单点变异和在N-端或C-端插入单个甘氨酸。由于宿主和客体之间大量的互补相互作用，生物肽(β-淀粉样肽)提供了更强的结合(几十纳摩尔)，为广泛的生物应用打开了大门。
A general method for peptide recognition has been elusive despite decades of research. Strong binding and selectivity among closely related peptides are necessary for biological applications but have been difficult to achieve with synthetic receptors. With inspiration from highly specific protein-protein and protein-ligand interactions, protein sized, water-soluble imprinted nanoparticles were prepared via templated polymerization of peptides within cross-linked micelles. Combination of hydrophobic and polar interactions afforded micromolar to submicromolar binding affinities for selected tripeptides. A "golden pair" of functional monomers was identified to enhance both the affinity and selectivity of binding and enabled differentiation of subtly different sequences including single-point variation of lysine by arginine and insertion of a single glycine at the N- or C-terminus. Biological peptides (beta-amyloid peptides) afforded even stronger binding (tens of nanomolar) due to a larger number of complementary interactions between the host and the guest, opening doors to a wide range of biological applications.