Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different.
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 3725627
Author(s) Seuring, Carolin; Verasdonck, Joeri; Ringler, Philippe; Cadalbert, Riccardo; Stahlberg, Henning; Böckmann, Anja; Meier, Beat H; Riek, Roland
Author(s) at UniBasel Stahlberg, Henning
Year 2017
Title Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different.
Journal The journal of physical chemistry. B
Volume 121
Number 8
Pages / Article-Number 1783-1792
Abstract

Amyloid polymorphism of twisted and straight β-endorphin fibril was studied by negative-stain transmission electron microscopy, scanning transmission electron microscopy, and solid-state nuclear magnetic resonance spectroscopy. While fibrils assembled in the presence of salt form flat, striated ribbons, in the absence of salt they formed mainly twisted filaments. To get insights into their structural differences at the atomic level, 3D solid-state NMR spectra on both fibril types were acquired allowing the detection of the differences in chemical shifts of 13C and 15N atoms in both preparations. The spectral fingerprints and therefore the chemical shifts are very similar for both fibril types. This indicates that the monomer structure and the molecular interfaces are almost the same but that these small differences do propagate to produce flat and twisted morphologies at the mesoscopic scale.

ISSN/ISBN 1520-5207
Full Text on edoc
Digital Object Identifier DOI 10.1021/acs.jpcb.6b10624
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/28075583
   

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