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Identification of Core Segment of Amyloidal Peptide Mediated by Chaperone Molecules by using Scanning Tunneling Microscopy
Author(s) -
Yu Yue,
Yang Yanlian,
Wang Chen
Publication year - 2015
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201500340
Subject(s) - peptide , chaperone (clinical) , scanning tunneling microscope , lamellar structure , biophysics , molecule , chemistry , homogeneous , crystallography , nanotechnology , materials science , biochemistry , biology , physics , organic chemistry , medicine , pathology , thermodynamics
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.