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

Lin Niu; Lei Liu; Meng Xu; Jacob Cramer; Kurt V. Gothelf; Mingdong Dong; Flemming Besenbacher; Qingdao Zeng; Yanlian Yang; Chen Wang

doi:10.1039/C4CC02748E

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

Lin Niu,†^a Lei Liu,†^abc Meng Xu,^a Jacob Cramer,^b Kurt V. Gothelf,^b Mingdong Dong,^b Flemming Besenbacher,^b Qingdao Zeng,^a Yanlian Yang*^a and Chen Wang*^a

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* Corresponding authors

^a 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
E-mail: wangch@nanoctr.cn, yangyl@nanoctr.cn

^b Interdisciplinary Nanoscience Center, Aarhus University, DK-8000 Aarhus C, Denmark

^c Institute for Advanced Materials, Jiangsu University, China

Abstract

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.

This article is part of the themed collection: Scanning Probe Studies of Molecular Systems

Chemical Communications

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

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

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