Reference : Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amy...
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Multidisciplinary, general & others
Physics and Materials Science
Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals
Adamcik, Jozef [ETH Zürich]
Ruggeri, Francesco Simone [University of Cambridge]
Berryman, Josh mailto [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]
Advanced Science
[en] amyloid crystals ; amyloid fibrils ; amyloid polymorphism ; nanomechanical properties ; secondary structure
[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.
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

File(s) associated to this reference

Fulltext file(s):

Open access
advs.202002182.pdfPublisher postprint3.87 MBView/Open

Bookmark and Share SFX Query

All documents in ORBilu are protected by a user license.