ArticleRSC advances2019
Effect of the surface curvature on amyloid-β peptide adsorption for graphene.
Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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
4 citing papers in PubMed, 14 citations in OpenAlex.
- Exploring 2D Graphene-Based Nanomaterials for Biomedical Applications: A Theoretical Modeling Perspective.Small science · 2025Article
- Confinement and Polarity Effects on the Peptide Packing Density on Mesoporous Silica Nanoparticles.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- The Hybrid Nano-Biointerface between Proteins/Peptides and Two-Dimensional Nanomaterials.Molecules (Basel, Switzerland) · 2023Review
- Advanced nanomaterials for modulating Alzheimer's related amyloid aggregation.Nanoscale advances · 2022Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The adsorption of amyloid-β peptide (Aβ) onto graphene nanosheets with curvature at a neutral pH has been studied by using molecular dynamics simulations in combination with umbrella sampling. We found that Aβ adsorbed onto graphene with distinct characteristics, causing the breakage of hydrogen bonds which leads to its conformational change. Interestingly, the adsorption capacity of graphene's surface varies significantly depending on its curvature, namely, the surface with negative curvature has a higher probability to adsorb the Aβ than the one with positive curvature. This phenomenon is further evidenced by the binding energy between the complex of graphene and Aβ derived from the potential of mean force (PMF). The hydrophobic interactions and the direct dispersion interactions between the graphene nanosheet and the Aβ play a dominant role in the adsorption process. These findings indicate that not only is the chemical composition an important factor but also the shape of the nanoparticle is important in determining its interaction with proteins: the contacting surface curvature can lead to different adsorption capability.
Identifiers
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Registered trials
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