PAPER: Transformation of β-sheet structures of the amyloid peptide induced by molecular modulators

Niu L, Liu L, Xu M, Cramer J, Gothelf KV, Dong M, Besenbacher F, Zeng Q, Yang Y, Wang C.
Chem. Commun. (Camb), 2014 Aug 18;50(64):8923-6. doi: 10.1039/c4cc02748e.
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.


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.

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