ArticleThe Journal of biological chemistry2016
Flexibility and Solvation of Amyloid-β Hydrophobic Core.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
37 citing papers in PubMed, 47 citations in OpenAlex.
- Hydration water dynamics in amyloid-β aggregates using deuterium and oxygen-17 solid-state NMR spectroscopy.The Journal of chemical physics · 2026Article
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- Dynamics studies of side-chains and hydration shells in amyloid-β fibrils using deuterium and oxygen-17 solid-state NMR.Methods in enzymology · 2026Review
- Peptide-Based Therapeutics for Alzheimer's Disease: Medicinal Chemistry, AI-Guided Computational Design, and Blood-Brain Barrier Delivery.Drug design, development and therapy · 2026Review
- Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024Article
- Raman Spectroscopic Insights of Phase-Separated Insulin Aggregates.ACS physical chemistry Au · 2024Article
- Analytical Framework to Understand the Origins of Methyl Side-Chain Dynamics in Protein Assemblies.Journal of the American Chemical Society · 2024Article
- Persistence of Methionine Side Chain Mobility at Low Temperatures in a Nine-Residue Low Complexity Peptide, as Probed byChemphyschem : a European journal of chemical physics and physical chemistry · 2024Article
- Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles.Physical chemistry chemical physics : PCCP · 2024Article
- Deuteron off-resonance rotating frame relaxation for the characterization of slow motions in rotating and static solid-state proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Effect of Cross-Seeding of Wild-Type Amyloid-βThe journal of physical chemistry. B · 2023Article
- Light, Water, and Melatonin: The Synergistic Regulation of Phase Separation in Dementia.International journal of molecular sciences · 2023Review
- The N-Terminal Domain of AβThe journal of physical chemistry. B · 2022Article
- Comparative Hydrophobic Core Dynamics Between Wild-Type Amyloid-β Fibrils, Glutamate-3 Truncation, and Serine-8 Phosphorylation.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022Article
- Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-β fibrils.Magnetic resonance in chemistry : MRC · 2021Article
- Irradiation effect of a submillimeter wave from 420 GHz gyrotron on amyloid peptides in vitro.Biomedical optics express · 2020Article
- Development of novelRSC advances · 2020Article
- Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020Review
- Deuteron Quadrupolar Chemical Exchange Saturation Transfer (Q-CEST) Solid-State NMR for Static Powder Samples: Approach and Applications to Amyloid-β Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Local ordering and dynamics in anisotropic media by magnetic resonance: from liquid crystals to proteins.Liquid crystals · 2020Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
Abstract
Amyloid fibril deposits found in Alzheimer disease patients are composed of amyloid-β (Aβ) protein forming a number of hydrophobic interfaces that are believed to be mostly rigid. We have investigated the μs-ms time-scale dynamics of the intra-strand hydrophobic core and interfaces of the fibrils composed of Aβ1-40 protein. Using solid-state (2)H NMR line shape experiments performed on selectively deuterated methyl groups, we probed the 3-fold symmetric and 2-fold symmetric polymorphs of native Aβ as well as the protofibrils of D23N Iowa mutant, associated with an early onset of Alzheimer disease. The dynamics of the hydrophobic regions probed at Leu-17, Leu-34, Val-36, and Met-35 side chains were found to be very pronounced at all sites and in all polymorphs of Aβ, with methyl axis motions persisting down to 230-200 K for most of the sites. The dominant mode of motions is the rotameric side chain jumps, with the Met-35 displaying the most complex multi-modal behavior. There are distinct differences in the dynamics among the three protein variants, with the Val-36 site displaying the most variability. Solvation of the fibrils does not affect methyl group motions within the hydrophobic core of individual cross-β subunits but has a clear effect on the motions at the hydrophobic interface between the cross-β subunits, which is defined by Met-35 contacts. In particular, hydration activates transitions between additional rotameric states that are not sampled in the dry protein. Thus, these results support the existence of water-accessible cavity recently predicted by molecular dynamics simulations and suggested by cryo-EM studies.
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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.