Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures
Controlled self-assembly of amphiphilic oligopeptides into shape-specific nanoarchitectures
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DOI：
10.1002/chem.200500611
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发表时间：
2006-02-01
影响因子：
4.3
通讯作者：
Higashi, N
中科院分区：
文献类型：
--
作者：
Koga, T;Higuchi, M;Higashi, N
在这里，我们报告了一种新的，可编程的，分子自组装系统，以制造特定形状的，三维纳米结构。制备了三种类型的由疏水性Leu和亲水性Lys组成的简单16-mer肽，LKL 16，KLK 16和LK 16，作为纳米纤维的构建块。利用圆二色谱（M）、傅立叶变换红外光谱（FTIR）和原子力显微镜（AFM）对分子的构象和自组装机理进行了详细的分析。通过调节肽序列、反应时间和溶液pH，可以制造各种各样的自组装纳米结构，例如β-片层、β-片层纤维、α-螺旋颗粒和α-螺旋片层。控制自组装纳米结构的能力应该提供对肽聚集机制的简单和/或基本的了解，包括淀粉样蛋白形成，这对新型生物相关纳米材料的设计将是有用的。
Here, we report a novel, programmable, molecular self-assembling system to fabricate shape-specific, three-dimensional nanoarchitectures. Three types of simple 16-mer peptides consisting of hydrophobic Leu and hydrophilic Lys, LKL16, KLK16, and LK16, were prepared as building blocks for nanofabrications. A detailed analysis of the conformation and self-assembling mechanism was performed by using circular dichroism (M), FTIR spectroscopy, and atomic force microscopy (AFM). A wide variety of self-assembled nanoarchitectures, such as beta-sheet-plates, beta-sheet-fibers, alpha-helix-particles, and alpha-helix-plates, could be fabricated by tuning the peptide sequence, reaction time, and solution pH. The ability to control the self-assembled nanostructures should provide a simple and/or essential insight into the mechanism of peptide aggregation, including amyloid formation, and it should be useful for the design of novel bio-related nanomaterials.