ArticleRoyal Society open science2017
A mix-and-click method to measure amyloid-β concentration with sub-micromolar sensitivity.
Article in Royal Society open science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 12 citations in OpenAlex.
- Theranostic Nanoparticles for Fluorosensitive Visualization and Inhibition of Amyloid Beta-Induced Neuroinflammation.Particle & particle systems characterization : measurement and description of particle properties and behavior in powders and other disperse systems · 2026Article
- N-Alkylamino Stilbene Compounds as Amyloid β Inhibitors for Alzheimer's Disease Research.Molecules (Basel, Switzerland) · 2025Article
- Nanotechnology for microglial targeting and inhibition of neuroinflammation underlying Alzheimer's pathology.Translational neurodegeneration · 2024Article
- Preparation and Fractionation of Heterogeneous Aβ42 Oligomers with Different Aggregation Properties.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Lipid membranes induce structural conversion from amyloid oligomers to fibrils.Biochemical and biophysical research communications · 2021Article
- Segmental structural dynamics in Aβ42 globulomers.Biochemical and biophysical research communications · 2021Article
- Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions.Biochemical and biophysical research communications · 2021Article
- Distinguishing the Effect on the Rate and Yield of Aβ42 Aggregation by Green Tea Polyphenol EGCG.ACS omega · 2020Article
- Early Effects of Aβ Oligomers on Dendritic Spine Dynamics and Arborization in Hippocampal Neurons.Frontiers in synaptic neuroscience · 2020Article
- Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism.Royal Society open science · 2019Article
- A mix-and-click method to measure amyloid-β concentration with sub-micromolar sensitivity.Royal Society open science · 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
5 authors at 1 institution in 1 country.
Funding
Abstract
Aggregation of amyloid-β (Aβ) protein plays a central role in Alzheimer's disease. Because protein aggregation is a concentration-dependent process, rigorous investigations require accurate concentration measurements. Owing to the high aggregation propensity of Aβ protein, working solutions of Aβ are typically in the low micromolar range. Therefore, an ideal Aβ quantification method requires high sensitivity without sacrificing speed and accuracy. Absorbance at 280 nm is frequently used to measure Aβ concentration, but the sensitivity is low with only one tyrosine and no tryptophan residues in the Aβ sequence. Here we present a fluorescence method for Aβ quantification using fluorescamine, which gives high fluorescence upon reaction with primary amines. We show that, using hen egg white lysozyme as a standard, fluorescence correlates linearly with primary amine concentration across a wide range of fluorescamine concentrations, from 62.5 to 1000 µM. The maximal sensitivity of detection is achieved at a fluorescamine concentration of 250 µM or higher. The fluorescamine method is compatible with the presence of dimethyl sulfoxide, which is commonly used in the preparation of Aβ oligomers, and limits the use of absorbance at 280 nm due to its high background reading. Using aggregation kinetics, we show that the fluorescamine method gives accurate concentration measurements at low micromolar range and leads to highly consistent aggregation data. We recommend the fluorescamine assay to be used for routine and on-the-fly concentration determination in Aβ oligomerization and fibrillization experiments.
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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.