Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides

Nicholas P. Reynolds, Jozef Adamcik, Joshua T. Berryman, Stephan Handschin, Ali Asghar Hakami Zanjani, Wen Li, Kun Liu, Afang Zhang and Raffaele Mezzenga ()
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Nicholas P. Reynolds: ARC Training Centre for Biodevices, Faculty of Science, Engineering and Technology
Jozef Adamcik: ETH Zurich, Department of Health Sciences & Technology
Joshua T. Berryman: University of Luxembourg, Department of Physics and Materials Science
Stephan Handschin: ETH Zurich, Department of Health Sciences & Technology
Ali Asghar Hakami Zanjani: University of Luxembourg, Department of Physics and Materials Science
Wen Li: Shanghai University, Department of Polymer Materials
Kun Liu: Shanghai University, Department of Polymer Materials
Afang Zhang: Shanghai University, Department of Polymer Materials
Raffaele Mezzenga: ETH Zurich, Department of Health Sciences & Technology

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract 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.

Date: 2017
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DOI: 10.1038/s41467-017-01424-4

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