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Surface-Assisted Assembly of an Ionic-Complementary Peptide: Controllable Growth of Nanofibers

机译:离子互补肽的表面辅助组装:纳米纤维的可控生长。

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摘要

Numerous studies have shown that a surface can direct and regulate molecular assembly. In this study, the nanofiber growth of an ionic-complementary peptide, EAK16-Ⅱ, on a mica surface was investigated under various solution conditions via in situ atomic force microscopy. In comparison to the assembly in bulk solution, nanofiber growth of EAK16-Ⅱ on mica is surface-assisted and involves two steps: (1) adsorption of nanofibers and fiber clusters (from the bulk solution) on the surface, serving as the "seeds"; (2) fiber elongation of the "seeds" from their active ends. The nanofiber growth can be controlled by adjusting the solution pH since it modulates the adsorption of the "seeds" on mica and their growth rates. The amount of the adsorbed "seeds" decreases with increasing solution pH, while the growth rate under different solution conditions is found to follow the order pure water > 1 mM HCl > 1 mM NaOH > 10 mM HCI ≈ 10 mM NaOH ≈ 0. The pH-dependent nanofiber growth is due to the surface charge of the peptides and peptide assemblies in various solutions as indicated by ζ-potential measurements. A simple model was proposed to describe surface-assisted nanofiber growth. This study provides insights into the assembly of peptide/protein on a surface, which is essential to understand such physiological protein aggregation systems as amyloid fibrillogenesis. In addition, the potential of this finding to construct biocompatible electrodes for biomolecular sensing is also discussed.
机译:大量研究表明,表面可以引导和调节分子组装。在这项研究中,通过原位原子力显微镜研究了在各种溶液条件下离子互补肽EAK16-Ⅱ在云母表面的纳米纤维生长。与在散装溶液中组装相比,EAK16-Ⅱ在云母上的纳米纤维生长是表面辅助的,包括两个步骤:(1)将纳米纤维和纤维团簇(来自散装溶液)吸附在表面上,作为“种子” “; (2)“种子”从其活动末端的纤维伸长率。可以通过调节溶液的pH值来控制纳米纤维的生长,因为它可以调节“种子”在云母上的吸附及其生长速率。随着溶液pH值的增加,吸附的“种子”的数量减少,而在不同溶液条件下的生长速率遵循以下顺序:纯水> 1 mM HCl> 1 mM NaOH> 10 mM HCl≈10 mM NaOH≈0。 pH依赖性纳米纤维的生长归因于ζ电位测量所显示的各种溶液中肽和肽装配体的表面电荷。提出了一个简单的模型来描述表面辅助纳米纤维的生长。这项研究提供了对肽/蛋白质在表面上组装的见解,这对于理解诸如淀粉样蛋白原纤维形成的生理蛋白质聚集系统是必不可少的。此外,还讨论了这一发现为生物分子传感构建生物相容性电极的潜力。

著录项

  • 来源
    《Journal of the American Chemical Society》 |2007年第40期|12200-12210|共11页
  • 作者单位

    Contribution from the Department of Chemical Engineering, University of Waterloo, 200 University Avenue West, Waterloo, Ontario N2L 3G1, Canada;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
  • 关键词

  • 入库时间 2022-08-18 03:21:33

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