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Title: Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates

Abstract

Various structural models for amyloid β fibrils have been derived from a variety of experimental techniques. However, these models cannot differentiate between the relative position of the two arms of the β hairpin called the stagger. Amyloid fibrils of various hierarchical levels form left-handed helices composed of β sheets. However it is unclear if positive, negative and zero staggers all form the macroscopic left-handed helices. To address this issue we have conducted extensive molecular dynamics simulations of amyloid β sheets of various staggers and shown that only negative staggers lead to the experimentally observed left-handed helices while positive staggers generate the incorrect right-handed helices. In conclusion, this result suggests that the negative staggers are physiologically relevant structure of the amyloid β fibrils.

Authors:
 [1];  [1];  [2]
+ Show Author Affiliations
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Computational Biology and Bioinformatics Group; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center; Univ. of Tennessee, Knoxville, TN (United States). Dept. of Biochemistry and Cellular and Molecular Biology; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). UT/ORNL Center for Molecular Biophysics
Publication Date:
Research Org.:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). BioEnergy Science Center (BESC)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1327590
Grant/Contract Number:  
AC05-00OR22725; AC02-05CH11231
Resource Type:
Accepted Manuscript
Journal Name:
FEBS Letters
Additional Journal Information:
Journal Volume: 587; Journal Issue: 16; Journal ID: ISSN 0014-5793
Publisher:
Federation of European Biochemical Societies
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; Amyloid; Alzheimer's; Protein structure

Citation Formats

GhattyVenkataKrishna, Pavan K., Uberbacher, Edward C., and Cheng, Xiaolin. Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates. United States: N. p., 2013. Web. doi:10.1016/j.febslet.2013.06.050.
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GhattyVenkataKrishna, Pavan K., Uberbacher, Edward C., & Cheng, Xiaolin. Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates. United States. https://doi.org/10.1016/j.febslet.2013.06.050
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GhattyVenkataKrishna, Pavan K., Uberbacher, Edward C., and Cheng, Xiaolin. Mon . "Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates". United States. https://doi.org/10.1016/j.febslet.2013.06.050. https://www.osti.gov/servlets/purl/1327590.
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@article{osti_1327590,
title = {Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates},
author = {GhattyVenkataKrishna, Pavan K. and Uberbacher, Edward C. and Cheng, Xiaolin},
abstractNote = {Various structural models for amyloid β fibrils have been derived from a variety of experimental techniques. However, these models cannot differentiate between the relative position of the two arms of the β hairpin called the stagger. Amyloid fibrils of various hierarchical levels form left-handed helices composed of β sheets. However it is unclear if positive, negative and zero staggers all form the macroscopic left-handed helices. To address this issue we have conducted extensive molecular dynamics simulations of amyloid β sheets of various staggers and shown that only negative staggers lead to the experimentally observed left-handed helices while positive staggers generate the incorrect right-handed helices. In conclusion, this result suggests that the negative staggers are physiologically relevant structure of the amyloid β fibrils.},
doi = {10.1016/j.febslet.2013.06.050},
journal = {FEBS Letters},
number = 16,
volume = 587,
place = {United States},
year = {Mon Jul 08 00:00:00 EDT 2013},
month = {Mon Jul 08 00:00:00 EDT 2013}
}
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journal, January 2007

Structure and Dynamics of Parallel β-Sheets, Hydrophobic Core, and Loops in Alzheimer’s Aβ Fibrils
journal, May 2007

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    • Katyal, Nidhi; Deep, Shashank
    • Physical Chemistry Chemical Physics, Vol. 21, Issue 44
    • DOI: 10.1039/c9cp03763b
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