ArticleRSC advances2015
Contrasting effects of nanoparticle-protein attraction on amyloid aggregation.
Article in RSC advances, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 63 citations in OpenAlex.
- Exploring Abeta42 monomer diffusion dynamics on fibril surfaces through molecular simulations.Protein science : a publication of the Protein Society · 2025Article
- Nanoplastic Stimulates the Amyloidogenesis of Parkinson's Alpha-Synuclein NACore.Small (Weinheim an der Bergstrasse, Germany) · 2024Article
- Nanocellulose aerogels as 3D amyloid templates.Nanoscale · 2023Article
- Deconstructing Electrostatics of Functionalized Metal Nanoparticles from Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- Aggregation of an Amyloidogenic Peptide on Gold Surfaces.Biomolecules · 2023Article
- Aggregation behavior of nanoparticles: Revisiting the phase diagram of colloids.Frontiers in molecular biosciences · 2022Review
- Organic dots (O-dots) for theranostic applications: preparation and surface engineering.RSC advances · 2021Review
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- On the Conformational Dynamics of β-Amyloid Forming Peptides: A Computational Perspective.Frontiers in bioengineering and biotechnology · 2020Review
- Morphological Determinants of Carbon Nanomaterial-Induced Amyloid Peptide Self-Assembly.Frontiers in chemistry · 2020Article
- Computational screening of nanoparticles coupling to Aβ40 peptides and fibrils.Scientific reports · 2019Article
- Amphiphilic surface chemistry of fullerenols is necessary for inhibiting the amyloid aggregation of alpha-synuclein NACore.Nanoscale · 2019Article
- Distinct Binding Dynamics, Sites and Interactions of Fullerene and Fullerenols with Amyloid-β Peptides Revealed by Molecular Dynamics Simulations.International journal of molecular sciences · 2019Article
- Building Minimalist Models for Functionalized Metal Nanoparticles.Frontiers in molecular biosciences · 2019Article
- Chaperone Like Attributes of Biogenic Fluorescent Gold Nanoparticles: Potential to Alleviate Toxicity Induced by Intermediate State Fibrils Against Neuroblastoma Cells.Frontiers in chemistry · 2019Article
- Article
- Mitigating Human IAPP Amyloidogenesis In Vivo with Chiral Silica Nanoribbons.Small (Weinheim an der Bergstrasse, Germany) · 2018Article
- Structures and dynamics of β-barrel oligomer intermediates of amyloid-beta16-22 aggregation.Biochimica et biophysica acta. Biomembranes · 2018Article
- Star Polymers Reduce Islet Amyloid Polypeptide Toxicity via Accelerated Amyloid Aggregation.Biomacromolecules · 2017Article
- Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide.Physical chemistry chemical physics : PCCP · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Nanoparticles (NPs) have been experimentally found to either promote or inhibit amyloid aggregation of proteins, but the molecular mechanisms for such complex behaviors remain unknown. Using coarse-grained molecular dynamics simulations, we investigated the effects of varying the strength of nonspecific NP-protein attraction on amyloid aggregation of a model protein, the amyloid-beta peptide implicated in Alzheimer's disease. Specifically, with increasing NP-peptide attraction, amyloid aggregation on the NP surface was initially promoted due to increased local protein concentration on the surface and destabilization of the folded state. However, further increase of NP-peptide attraction decreased the stability of amyloid fibrils and reduced their lateral diffusion on the NP surface necessary for peptide conformational changes and self-association, thus prohibiting amyloid aggregation. Moreover, we found that the relative concentration between protein and NPs also played an important role in amyloid aggregation. With a high NP/protein ratio, NPs that intrinsically promote protein aggregation may display an inhibitive effect by depleting the proteins in solution while having a low concentration of the proteins on each NP's surface. Our coarse-grained molecular dynamics simulation study offers a molecular mechanism for delineating the contrasting and seemingly conflicting effects of NP-protein attraction on amyloid aggregation and highlights the potential of tailoring anti-aggregation nanomedicine against amyloid diseases.
Identifiers
What OpenQuestion holds
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.