Bortolini Christian, Liu Lei, Gronewold Thomas M A, Wang Chen, Besenbacher Flemming, Dong Mingdong
Interdisciplinary Nanoscience Center (iNANO), Gustav Wieds 14, Building 1590, Aarhus C., Denmark.
Soft Matter. 2014 Aug 21;10(31):5656-61. doi: 10.1039/c4sm01065e. Epub 2014 Jul 4.
The final structure and properties of synthetic peptides mainly depend on their sequence composition and experimental conditions. This work demonstrates that a variation in the positions of hydrophobic residues within a peptide sequence can tune the self-assembly. Techniques employed are atomic force microscopy, transmission electron microscopy and an innovative method based on surface acoustic waves. In addition, a systematic investigation on pH dependence was carried out by utilizing constant experimental parameters.
合成肽的最终结构和性质主要取决于其序列组成和实验条件。这项工作表明，肽序列中疏水残基位置的变化可以调节自组装。所采用的技术有原子力显微镜、透射电子显微镜以及一种基于表面声波的创新方法。此外，通过利用恒定的实验参数对pH依赖性进行了系统研究。
