title: Transformation of β-sheet structures of the amyloid peptide induced by molecular modulators.
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.
authors: 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. wangch@nanoctr.cn yangyl@nanoctr.cn.
authors: Lin
authors: L
authors: Niu
authors: Lei
authors: L
authors: Liu
authors: Meng
authors: M
authors: Xu
authors: Jacob
authors: J
authors: Cramer
authors: Kurt V
authors: KV
authors: Gothelf
authors: Mingdong
authors: M
authors: Dong
authors: Flemming
authors: F
authors: Besenbacher
authors: Qingdao
authors: Q
authors: Zeng
authors: Yanlian
authors: Y
authors: Yang
authors: Chen
authors: C
authors: Wang
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D016252:Microscopy, Scanning Tunneling; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011725:Pyridines / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D011725:Pyridines; C529399:amyloid beta-protein (16-20)