ArticlePLoS computational biology2015
Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways.
Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- In silico peptide self-assembly reveals the importance of N-terminal motifs and the inhibition mechanism of the mutation L38M in α-synuclein fibrillation.Protein science : a publication of the Protein Society · 2026Article
- K16F/E22F Mutation Promotes Oligomerization and Alters β-Sheet Topology of Aβ16-22 Peptides: Insights from Molecular Dynamics Simulations.ACS chemical neuroscience · 2026Article
- Diverse Aggregation Kinetics Predicted by a Coarse-Grained Peptide Model.The journal of physical chemistry. B · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Disclosing the Interaction of Gold Nanoparticles with Aβ(1-40) Monomers through Replica Exchange Molecular Dynamics Simulations.International journal of molecular sciences · 2020Article
- The metastable states of proteins.Protein science : a publication of the Protein Society · 2020Review
- Is the p3 Peptide (Aβ17-40, Aβ17-42) Relevant to the Pathology of Alzheimer's Disease?1.Journal of Alzheimer's disease : JAD · 2020Review
- Recent Advances in Coarse-Grained Models for Biomolecules and Their Applications.International journal of molecular sciences · 2019Review
- Molecular insights into the surface-catalyzed secondary nucleation of amyloid-βScience advances · 2019Article
- Thermodynamic phase diagram of amyloid-β (16-22) peptide.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Assembly Mechanism for Aggregation of Amyloid Fibrils.International journal of molecular sciences · 2018Article
- Seeding and cross-seeding fibrillation of N-terminal prion protein peptides PrP(120-144).Protein science : a publication of the Protein Society · 2018Article
- Simulations and Experiments Delineate Amyloid Fibrilization by Peptides Derived from Glaucoma-Associated Myocilin.The journal of physical chemistry. B · 2018Article
- Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid β Assemblies.International journal of molecular sciences · 2018Article
- Article
- Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide.Physical chemistry chemical physics : PCCP · 2017Article
- Polymorphism of fibrillar structures depending on the size of assembled AβScientific reports · 2016Article
- N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways.The Journal of biological chemistry · 2016Article
- Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation.The journal of physical chemistry. B · 2016Article
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3 authors.
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Abstract
Discovering the mechanisms by which proteins aggregate into fibrils is an essential first step in understanding the molecular level processes underlying neurodegenerative diseases such as Alzheimer's and Parkinson's. The goal of this work is to provide insights into the structural changes that characterize the kinetic pathways by which amyloid-β peptides convert from monomers to oligomers to fibrils. By applying discontinuous molecular dynamics simulations to PRIME20, a force field designed to capture the chemical and physical aspects of protein aggregation, we have been able to trace out the entire aggregation process for a system containing 8 Aβ17-42 peptides. We uncovered two fibrillization mechanisms that govern the structural conversion of Aβ17-42 peptides from disordered oligomers into protofilaments. The first mechanism is monomeric conversion templated by a U-shape oligomeric nucleus into U-shape protofilament. The second mechanism involves a long-lived and on-pathway metastable oligomer with S-shape chains, having a C-terminal turn, en route to the final U-shape protofilament. Oligomers with this C-terminal turn have been regarded in recent experiments as a major contributing element to cell toxicity in Alzheimer's disease. The internal structures of the U-shape protofilaments from our PRIME20/DMD simulation agree well with those from solid state NMR experiments. The approach presented here offers a simple molecular-level framework to describe protein aggregation in general and to visualize the kinetic evolution of a putative toxic element in Alzheimer's disease in particular.
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