ArticleJournal of molecular biology2018
Nanodisc-Forming Scaffold Protein Promoted Retardation of Amyloid-Beta Aggregation.
Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 60 citations in OpenAlex.
- Molecular Mechanisms Governing Peptide Nanodisc Assembly and Stability.bioRxiv : the preprint server for biology · 2026Article
- The HDL-Mimetic Peptide 4F Mitigates Vascular and Cortical Amyloid Pathology and Associated Neuroinflammation in a Transgenic Mouse Model of Cerebral Amyloid Angiopathy and Alzheimer's Disease.Molecular neurobiology · 2025Article
- Di-caffeoylquinic acid: a potential inhibitor for amyloid-beta aggregation.Journal of natural medicines · 2024Article
- Review
- Vav2 is a novel APP-interacting protein that regulates APP protein level.Scientific reports · 2022Article
- Conformational Tuning of Amylin by Charged Styrene-Maleic-Acid Copolymers.Journal of molecular biology · 2022Article
- Inhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles.Chemistry of materials : a publication of the American Chemical Society · 2021Article
- Solid-State NMR Study to Probe the Effects of Divalent Metal Ions (CaLangmuir : the ACS journal of surfaces and colloids · 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
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins.ACS chemical neuroscience · 2020Article
- Amyloidosis Inhibition, a New Frontier of the Protein Corona.Nano today · 2020Article
- Time-Dependent Lipid Dynamics, Organization and Peptide-Lipid Interaction in Phospholipid Bilayers with Incorporated β-Amyloid Oligomers.The journal of physical chemistry letters · 2020Article
- Ion channel formation by N-terminally truncated Aβ (4-42): relevance for the pathogenesis of Alzheimer's disease.Nanomedicine : nanotechnology, biology, and medicine · 2020Article
- Molecular chirality mediated amyloid formation on phospholipid surfaces.Chemical science · 2020Article
- High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways.International journal of molecular sciences · 2020Review
- High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease.Chemical communications (Cambridge, England) · 2020Review
- Structural Interaction of Apolipoprotein A-I Mimetic Peptide with Amyloid-β Generates Toxic Hetero-oligomers.Journal of molecular biology · 2020Article
- Acetylation of AβACS chemical neuroscience · 2020Article
- Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide.Nano letters · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Peptidic nanodiscs are useful membrane mimetic tools for structural and functional studies of membrane proteins, and membrane interacting peptides including amyloids. Here, we demonstrate anti-amyloidogenic activities of a nanodisc-forming 18-residue peptide (denoted as 4F), both in lipid-bound and lipid-free states by using Alzheimer's amyloid-beta (Aβ40) peptide as an example. Fluorescence-based amyloid fibrillation kinetic assays showed a significant delay in Aβ40 amyloid aggregation by the 4F peptide. In addition, 4F-encased lipid nanodiscs, at an optimal concentration of 4F (>20 μM) and nanodisc size (<10 nm), significantly affect amyloid fibrillation. A comparison of experimental results obtained from nanodiscs with that obtained from liposomes revealed a substantial inhibitory efficacy of 4F-lipid nanodiscs against Aβ40 aggregation and were also found to be suitable to trap Aβ40 intermediates. A combination of atomistic molecular dynamics simulations with NMR and circular dichroism experimental results exhibited a substantial change in Aβ40 conformation upon 4F binding through electrostatic and π-π interactions. Specifically, the 4F peptide was found to interfere with the central β-sheet-forming residues of Aβ40 through substantial hydrogen, π-π, and π-alkyl interactions. Fluorescence experiments and coarse-grained molecular dynamics simulations showed the formation of a ternary complex, where Aβ40 binds to the proximity of peptidic belt and membrane surface that deaccelerate amyloid fibrillation. Electron microscopy images revealed short and thick amyloid fibers of Aβ40 formed in the presence of 4F or 4F-lipid nanodsics. These findings could aid in the development of amyloid inhibitors as well as in stabilizing Aβ40 intermediates for high-resolution structural and neurobiological 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.