ArticleACS omega2020
Adsorption of Amyloid Beta Peptide by Metal-Organic Frameworks.
Article in ACS omega, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Protein adsorption at material interface: mechanistic design framework for engineering ceramic scaffolds for bone repair applications.Biomedical engineering online · 2026Review
- Nanomaterials that Aid in the Diagnosis and Treatment of Alzheimer's Disease, Resolving Blood-Brain Barrier Crossing Ability.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Synergistic effect of hierarchical topographic structure on 3D-printed Titanium scaffold for enhanced coupling of osteogenesis and angiogenesis.Materials today. Bio · 2023Article
- Phosphorylation of covalent organic framework nanospheres for inhibition of amyloid-β peptide fibrillation.Chemical science · 2022Article
- Layered Double Hydroxide@Metal-Organic Framework Hybrids for Extraction of Indole-3-Carbinol From Cruciferous Vegetables.Frontiers in nutrition · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metal-organic frameworks (MOFs) are capable of adsorbing a wide range of molecules. In addition to the more commonly investigated small molecules, researchers have demonstrated that MOFs adsorb much larger molecules, such as proteins and peptides. We have investigated whether MOFs are capable of adsorbing amyloid beta peptide. Amyloid beta plays a pivotal role in the progression of Alzheimer's disease because individual copies of the peptides can aggregate, forming neurotoxic oligomers and the amyloid plaques found in brains of Alzheimer's patients. After synthesizing a number of commonly studied MOFs, their adsorption capabilities were tested. We found that the MOFs tested readily adsorbed small amounts of amyloid beta (as determined by gel electrophoresis). It was determined that in most cases, adsorption occurs rapidly, with complete adsorption within minutes of incubation. Overall adsorption capacity was found to vary between different MOFs as well. Once adsorbed, amyloid beta peptide can subsequently be eluted from some MOFs by treatment with acetonitrile/water solutions, though retention strength varied between different MOFs. In some cases, MOFs that showed complete adsorption also saw high levels of peptide elution, but others showed little to no elution of the peptide. Together these data can help us begin to understand the interactions between amyloid beta and MOFs.
Identifiers
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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.