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A DFT‐Assisted Topological Analysis of Four Polymorphic, S‐Shaped Aβ42 Fibril Structures
Author(s) -
Foley Alejandro R.,
Raskatov Jevgenij A.
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900036
Subject(s) - fibril , amyloid fibril , peptide , computational biology , chemistry , amyloid β , biophysics , topology (electrical circuits) , nanotechnology , materials science , biology , disease , biochemistry , medicine , mathematics , pathology , combinatorics
Amyloid β 42 (Aβ42) is an inherently disordered peptide, whose toxic actions are believed to play important roles in the etiology of Alzheimer's disease. Four fibril structures of the peptide that display broadly similar characteristics were recently published, but a systematic comparison of these structures is lacking. In this paper, a topological framework was created to enable such understanding and produced new insights into subtle structural elements that underlie the overall structural diversity. A DFT‐based analysis illuminated some of the energetic differences that arise as a consequence.