Article (Scientific journals)
Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals
Adamcik, Jozef; Ruggeri, Francesco Simone; Berryman, Josh et al.
2020In Advanced Science, p. 2002182
Peer reviewed
 

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Keywords :
amyloid crystals; amyloid fibrils; amyloid polymorphism; nanomechanical properties; secondary structure
Abstract :
[en] Abstract Nanomechanical properties of amyloid fibrils and nanocrystals depend on their secondary and quaternary structure, and the geometry of intermolecular hydrogen bonds. Advanced imaging methods based on atomic force microscopy (AFM) have unravelled the morphological and mechanical heterogeneity of amyloids, however a full understanding has been hampered by the limited resolution of conventional spectroscopic methods. Here, it is shown that single molecule nanomechanical mapping and infrared nanospectroscopy (AFM-IR) in combination with atomistic modelling enable unravelling at the single aggregate scale of the morphological, nanomechanical, chemical, and structural transition from amyloid fibrils to amyloid microcrystals in the hexapeptides, ILQINS, IFQINS, and TFQINS. Different morphologies have different Young's moduli, within 2?6 GPa, with amyloid fibrils exhibiting lower Young's moduli compared to amyloid microcrystals. The origins of this stiffening are unravelled and related to the increased content of intermolecular ?-sheet and the increased lengthscale of cooperativity following the transition from twisted fibril to flat nanocrystal. Increased stiffness in Young's moduli is correlated with increased density of intermolecular hydrogen bonding and parallel beta-sheet structure, which energetically stabilize crystals over the other polymorphs. These results offer additional evidence for the position of amyloid crystals in the minimum of the protein folding and aggregation landscape.
Research center :
ULHPC - University of Luxembourg: High Performance Computing
Disciplines :
Physical, chemical, mathematical & earth Sciences: Multidisciplinary, general & others
Author, co-author :
Adamcik, Jozef;  ETH Zürich
Ruggeri, Francesco Simone;  University of Cambridge
Berryman, Josh  ;  University of Luxembourg > Faculty of Science, Technology and Medicine (FSTM) > Department of Physics and Materials Science (DPHYMS)
Zhang, Afang;  Shanghai University
Knowles, Tuomas P J;  University of Cambridge
Mezzenga, Raffaele;  ETH Zürich
External co-authors :
yes
Language :
English
Title :
Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals
Publication date :
2020
Journal title :
Advanced Science
Publisher :
Wiley
Pages :
2002182
Peer reviewed :
Peer reviewed
Focus Area :
Physics and Materials Science
FnR Project :
FNR8329720 - Assembly Kinetics And Phase Diagram Of A Lysozyme-derived Peptide, 2014 (01/09/2015-31/08/2018) - Joshua T Berryman
Name of the research project :
ILQINS
Funders :
FNR - Fonds National de la Recherche [LU]
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since 04 January 2021

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