ArticleThe journal of physical chemistry. B2018
Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.
Article in The journal of physical chemistry. B, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- Fragmentation-Induced Disassembly and Reaggregation of α-Synuclein Amyloid Fibrils.ACS chemical neuroscience · 2026Article
- Substituent-Based Modulation of Self-Assembly and Immunogenicity of Amphipathic Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Elucidating β-Sheet Ordering in Lipopeptides Bearing Lysine-Rich Tripeptide Sequences: Fibrils versus Nanotapes.The journal of physical chemistry. B · 2026Article
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- Structural Insights Into Amyloid Polymorphism: The Impact of Glutamine to Norleucine Substitutions in GNNQQNY Aggregation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Principles and Biomedical Applications of Self-Assembled Peptides: Potential Treatment of Type 2 Diabetes Mellitus.Pharmaceutics · 2024Review
- Rational Design of TDP-43 Derived α-Helical Peptide Inhibitors: AnACS chemical neuroscience · 2024Article
- Lipid-induced polymorphic amyloid fibril formation by α-synuclein.Protein science : a publication of the Protein Society · 2023Article
- New Insights into the Molecular Interplay between Human Herpesviruses and Alzheimer's Disease-A Narrative Review.Brain sciences · 2022Review
- Virtual Quasi-2D Intermediates as Building Blocks for Plausible Structural Models of Amyloid Fibrils from Proteins with Complex Topologies: A Case Study of Insulin.Langmuir : the ACS journal of surfaces and colloids · 2022Article
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- Amyloid β 42 fibril structure based on small-angle scattering.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.Computational and structural biotechnology journal · 2021Review
- Fibril Surface-Dependent Amyloid Precursors Revealed by Coarse-Grained Molecular Dynamics Simulation.Frontiers in molecular biosciences · 2021Article
- Atomistic fibrillar architectures of polar prion-inspired heptapeptides.Chemical science · 2020Article
- Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly.Communications chemistry · 2020Article
- Protofilament Structure and Supramolecular Polymorphism of Aggregated Mutant Huntingtin Exon 1.Journal of molecular biology · 2020Article
- Interactions between Curcumin Derivatives and Amyloid-β Fibrils: Insights from Molecular Dynamics Simulations.Journal of chemical information and modeling · 2020Article
- High Speed AFM and NanoInfrared Spectroscopy Investigation of AβFrontiers in molecular biosciences · 2020Article
- Surveying the Energy Landscapes of Aβ Fibril Polymorphism.The journal of physical chemistry. B · 2018Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Amyloid fibrils are highly ordered protein aggregates associated with more than 40 human diseases. The exact conditions under which the fibrils are grown determine many types of reported fibril polymorphism, including different twist patterns. Twist-based polymorphs display unique mechanical properties in vitro, and the relevance of twist polymorphism in amyloid diseases has been suggested. We present transmission electron microscopy images of Aβ42-derived (amyloid β) fibrils, which are associated with Alzheimer's disease, demonstrating the presence of twist variability even within a single long fibril. To better understand the molecular underpinnings of twist polymorphism, we present a structural and thermodynamics analysis of molecular dynamics simulations of the twisting of β-sheet protofilaments of a well-characterized cross-β model: the GNNQQNY peptide from the yeast prion Sup35. The results show that a protofilament model of GNNQQNY is able to adopt twist angles from -11° on the left-hand side to +8° on the right-hand side in response to various external conditions, keeping an unchanged peptide structure. The potential of mean force (PMF) of this cross-β structure upon twisting revealed that only ∼2k
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.