The Two-Step Assemblies of Basic-Amino-Acid-Rich Peptide with a Highly Charged Polyoxometalate
The Two-Step Assemblies of Basic-Amino-Acid-Rich Peptide with a Highly Charged Polyoxometalate
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富含碱性氨基酸的肽与高电荷多金属氧酸盐的两步组装
DOI：
10.1002/chem.201501243
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Lixin Wu
中科院分区：
文献类型：
--
作者：
Teng Zhang;Hong-Wei Li;Yuqing Wu;Yizhan Wang;Lixin Wu
报道了HPV16 L1的肽与高电荷的铕取代多金属氧酸盐（POM）簇的两步组装，并伴有无机多阴离子的发光增强。通过分析等温滴定量热法（ITC）、时间分辨荧光光谱和核磁共振光谱的热力学参数，详细讨论了其机理。通过比较肽类似物的作用，提出了相应的结合过程和模型。阐明了每个结合步骤的驱动力，并揭示了初始POM聚集，肽的基本序列和疏水C端对两步组装的本质贡献。本研究证明了一种有意义的生物无机材料制备方法，以及一种利用聚甲醛调节多肽甚至蛋白质组装的策略，这种方法可以通过利用具有相似性质的多肽和聚甲醛扩展到其他蛋白质和/或病毒。
Two‐step assembly of a peptide from HPV16 L1 with a highly charged europium‐substituted polyoxometalate (POM) cluster, accompanying a great luminescence enhancement of the inorganic polyanions, is reported. The mechanism is discussed in detail by analyzing the thermodynamic parameters from isothermal titration calorimetry (ITC), time‐resolved fluorescent and NMR spectra. By comparing the actions of the peptide analogues, a binding process and model are proposed accordingly. The driving forces in each binding step are clarified, and the initial POM aggregation, basic‐sequence and hydrophobic C termini of peptide are revealed to contribute essentially to the two‐step assembly. The present study demonstrates both a meaningful preparation for bioinorganic materials and a strategy using POMs to modulate the assembly of peptides and even proteins, which could be extended to other proteins and/or viruses by using peptides and POMs with similar properties.