Seki Takakazu, So Christopher R, Page Tamon R, Starkebaum David, Hayamizu Yuhei, Sarikaya Mehmet
Department of Materials Science and Engineering, Tokyo Institute of Technology , Tokyo 152-8550, Japan.
Genetically Engineered Materials Science and Engineering Center, Departments of Materials Science and Engineering and Chemical Engineering, University of Washington , Seattle, Washington 98195, United States.
Langmuir. 2018 Feb 6;34(5):1819-1826. doi: 10.1021/acs.langmuir.7b02231. Epub 2017 Nov 9.
The nanoscale self-organization of biomolecules, such as proteins and peptides, on solid surfaces under controlled conditions is an important issue in establishing functional bio/solid soft interfaces for bioassays, biosensors, and biofuel cells. Electrostatic interaction between proteins and surfaces is one of the most essential parameters in the adsorption and self-assembly of proteins on solid surfaces. Although the adsorption of proteins has been studied with respect to the electrochemical surface potential, the self-assembly of proteins or peptides forming well-organized nanostructures templated by lattice structure of the solid surfaces has not been studied in the relation to the surface potential. In this work, we utilize graphite-binding peptides (GrBPs) selected by the phage display method to investigate the relationship between the electrochemical potential of the highly ordered pyrolytic graphite (HOPG) and peptide self-organization forming long-range-ordered structures. Under modulated electrical bias, graphite-binding peptides form various ordered structures, such as well-ordered nanowires, dendritic structures, wavy wires, amorphous (disordered) structures, and islands. A systematic investigation of the correlation between peptide sequence and self-organizational characteristics reveals that the presence of the bias-sensitive amino acid modules in the peptide sequence has a significant effect on not only surface coverage but also on the morphological features of self-assembled structures. Our results show a new method to control peptide self-assembly by means of applied electrochemical bias as well as peptide design-rules for the construction of functional soft bio/solid interfaces that could be integrated in a wide range of practical implementations.
在可控条件下，蛋白质和肽等生物分子在固体表面的纳米级自组装是建立用于生物测定、生物传感器和生物燃料电池的功能性生物/固体软界面的重要问题。蛋白质与表面之间的静电相互作用是蛋白质在固体表面吸附和自组装中最关键的参数之一。尽管已针对电化学表面电位研究了蛋白质的吸附，但尚未研究蛋白质或肽以固体表面晶格结构为模板形成有序纳米结构的自组装与表面电位的关系。在这项工作中，我们利用通过噬菌体展示法筛选出的石墨结合肽（GrBPs）来研究高度有序热解石墨（HOPG）的电化学电位与形成长程有序结构的肽自组装之间的关系。在调制电偏压下，石墨结合肽形成各种有序结构，如有序纳米线、树枝状结构、波浪线、无定形（无序）结构和岛状结构。对肽序列与自组织特性之间相关性的系统研究表明，肽序列中对偏压敏感的氨基酸模块的存在不仅对表面覆盖率有显著影响，而且对自组装结构的形态特征也有显著影响。我们的结果展示了一种通过施加电化学偏压来控制肽自组装的新方法，以及构建功能性软生物/固体界面的肽设计规则，这些界面可集成到广泛的实际应用中。
