Niu Lin, Liu Lei, Xu Meng, Cramer Jacob, Gothelf Kurt V, Dong Mingdong, Besenbacher Flemming, Zeng Qingdao, Yang Yanlian, Wang Chen
Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety (Chinese Academy of Sciences), and Key Laboratory of Standardization and Measurement for Nanotechnology (Chinese Academy of Sciences), National Center for Nanoscience and Technology, Beijing 100190, China.
Chem Commun (Camb). 2014 Aug 18;50(64):8923-6. doi: 10.1039/c4cc02748e.
In this work we report the effect of terminus molecular modulators on the secondary structures of the amyloid peptide aggregates. The controlled modulation of the assembly structure and the transformation of β-sheet secondary structures could be beneficial for gaining insight into the aggregation mechanism of peptides. Particularly, multiple assembling characteristics have been identified as a reflection of peptide-organic interactions.
在这项工作中，我们报告了末端分子调节剂对淀粉样肽聚集体二级结构的影响。对组装结构的可控调节以及β-折叠二级结构的转变可能有助于深入了解肽的聚集机制。特别是，已确定多种组装特征反映了肽与有机物的相互作用。
