Reference : Amyloid Evolution: Antiparallel Replaced by Parallel
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Physical, chemical, mathematical & earth Sciences : Multidisciplinary, general & others
Physics and Materials Science; Computational Sciences
Amyloid Evolution: Antiparallel Replaced by Parallel
Hakami Zanjani, Ali Asghar mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > >]
Reynolds, Nicholas mailto [La Trobe University > La Trobe Institute for Molecular Science]
Zhang, Afang mailto [Shanghai University > Department of Polymer Materials]
Schilling, Tanja mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Physics and Materials Science Research Unit >]
Mezzenga, Raffaele mailto [ETH Zurich > Department of Health Sciences and Technology > > ; ETH Zurich > Department of Materials]
Berryman, Josh mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Physics and Materials Science Research Unit >]
Biophysical Journal
Biophysical Society
Yes (verified by ORBilu)
[en] amyloid ; simulation ; WAXS
[en] Several atomic structures have now been found for micrometer-scale amyloid fibrils or elongated microcrystals using a range of methods, including NMR, electron microscopy, and X-ray crystallography, with parallel beta-sheet appearing as the most common secondary structure. The etiology of amyloid disease, however, indicates nanometer-scale assemblies of only tens of peptides as significant agents of cytotoxicity and contagion. By combining solution X-ray with molecular dynamics, weshow that antiparallel structure dominates at the first stages of aggregation for a specific set of peptides, being replaced by parallel at large length scales only. This divergence in structure between small and large amyloid aggregates should inform future design of molecular therapeutics against nucleation or intercellular transmission of amyloid. Calculations and an overview from the literature argue that antiparallel order should be the first appearance of structure in many or most amyloid aggregation processes, regardless of the endpoint. Exceptions to this finding should exist, depending inevitably on the sequence and on solution conditions.
University of Luxembourg: High Performance Computing - ULHPC
Fonds National de la Recherche - FnR
Researchers ; Professionals ; Students ; General public
FnR ; FNR8329720 > Joshua T Berryman > ILQINS > ASSEMBLY KINETICS AND PHASE DIAGRAM OF A LYSOZYME-DERIVED PEPTIDE > 01/09/2015 > 31/08/2018 > 2014

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