Reference : Competition between crystal and fibril formation in molecular mutations of amyloidoge...
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Multidisciplinary, general & others
Physics and Materials Science
http://hdl.handle.net/10993/32910
Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
English
Reynolds, Nicholas [Swinburne University of Technology]
Adamcik, Jozef [ETH Zurich]
Berryman, Josh mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Physics and Materials Science Research Unit >]
Handschin, Stephan [ETH Zurich]
Hakami Zanjani, Ali Asghar mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Physics and Materials Science Research Unit >]
Li, Wen [Shanghai University]
Liu, Kun [Shanghai University]
Zhang, Afang [Shanghai University]
Mezzenga, Raffaele [ETH Zurich]
Nov-2017
Nature Communications
Springer-Nature
8
Yes (verified by ORBilu)
International
2041-1723
London
United Kingdom
[en] Biological Physics ; Peptides ; Protein Aggregation
[en] Amyloidogenic model peptides are invaluable for investigating assembly mechanisms in disease related amyloids and in protein folding. During aggregation, such peptides can undergo bifurcation leading to fibrils or crystals, however the mechanisms of fibril-to-crystal conversion are unclear. We navigate herein the energy landscape of amyloidogenic peptides by studying a homologous series of hexapeptides found in animal, human and disease related proteins. We observe fibril-to-crystal conversion occurring within single aggregates via untwisting of twisted ribbon fibrils possessing saddle-like curvature and cross-sectional aspect ratios approaching unity. Changing sequence, pH or concentration shifts the growth towards larger aspect ratio species assembling into stable helical ribbons possessing mean-curvature. By comparing atomistic calculations of desolvation energies for association of peptides we parameterise a kinetic model, providing a physical explanation of fibril-to-crystal interconversion. These results shed light on the self-assembly of amyloidogenic peptides, suggesting amyloid crystals, not fibrils, represent the ground state of the protein folding energy landscape.
University of Luxembourg: High Performance Computing - ULHPC
Australian Research Council ; National Natural Science Foundation of China ; Science and Industry Endowment Fund (SIEF) ; Fonds National de la Recherche - FnR
Researchers ; Professionals ; Students ; General public ; Others
http://hdl.handle.net/10993/32910
10.1038/s41467-017-01424-4
http://www.nature.com/articles/s41467-017-01424-4
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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