Identification of Core Segment of Amyloidal Peptide Mediated by Chaperone Molecules by using Scanning Tunneling Microscopy.
We illustrate in this work that pristine assemblies of amyloidal peptides can be obtained by perturbations of reduced scanning bias, and show a broad distribution in peptide length. In contrast, the chaperone-mediated peptide co-assembly presents ordered lamellar structures with a homogeneous distribution in length, which could be attributed to the core segment of the peptide. The efforts are beneficial for gaining insight into the aggregation propensity of peptides and inter-peptide interactions.
National Center for Nanoscience and Technology, Beijing 100190 (China).
Yue
Y
Yu
National Center for Nanoscience and Technology, Beijing 100190 (China).
Yanlian
Y
Yang
National Center for Nanoscience and Technology, Beijing 100190 (China). wangch@nanoctr.cn.
Chen
C
Wang
D058227:Amyloidogenic Proteins / Q000737:chemistry*; D016252:Microscopy, Scanning Tunneling; D018832:Molecular Chaperones / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
D058227:Amyloidogenic Proteins; D018832:Molecular Chaperones; D010455:Peptides
peptides; scanning tunneling microscopy; self-assembly; single-molecule studies; surface analysis