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Creative Biolabs

Amyloid-beta Aggregate Determination Assay Service

By detecting the various stages of amyloid-beta (Aβ) aggregates, researchers can more accurately assess the efficacy of potential therapeutic interventions and identify significant biomarkers for the development of novel drugs. For further information regarding the products and services provided, project-specific consultation, and pricing, please submit an inquiry here.

Introduction

Schematic representation of amyloid formation process. (Polanco, et al., 2022)

Aβ aggregates are a key pathological feature of neurodegenerative diseases such as Alzheimer's disease (AD). Studies have shown that Aβ peptides accumulate in the brain and form fibrillar aggregates that are toxic to neurons, leading to cognitive impairment and dementia. Accurate detection and analysis of Aβ aggregates is therefore critical to understanding their role in the disease.

Available Assays at Creative Biolabs

  • Aggregated Aβ Assay

Aβ monomers can self-assemble into low-molecular-weight oligomers, further form high-molecular-weight fibrillar structures, and finally deposit as amyloid plaques. Aβ aggregation is a dynamic process involving two stages: nucleation and polymerization, in which stable seeds (such as fibril fragments) serve as polymerization templates to accelerate aggregation. Our Aβ aggregation service is suitable for a variety of samples, including brain homogenate, cerebrospinal fluid, in vitro aggregated Aβ, and various cell culture samples.

For downstream detection, we can provide thioflavin T (ThT) or enzyme-linked immunosorbent assay (ELISA) based assays to detect the kinetics of Aβ aggregation.

ThT Assay

ThT is a commonly used dye that can specifically bind to amyloid fibrils and assess the formation of Aβ aggregates by monitoring changes in fluorescence intensity.

Fig 1: Linear correlation between ThT fluorescence intensity and amyloid fibril concentration. Fig.1 ThT fluorescence intensity correlated linearly with amyloid fibril concentration.2, 5

ELISA Assay

ELISA is commonly used to detect Aβ40 and Aβ42 aggregates by using specific antibodies to detect and quantify Aβ aggregates.

Fig 2: ELISA was used to analyze total and fibril levels of Aβ1-40 and Aβ1-42. Fig.2 Total and fibril levels of Aβ1-40 and Aβ1-42 were analyzed by ELISA.3, 5

  • Mass Spectrometry Analysis

Mass spectrometry can be used to identify and quantify the peptide composition of Aβ aggregates, helping to understand their structural and functional properties. Liquid chromatography-mass spectrometry can be used to analyze the composition of Aβ oligomers and fibers.

Fig 3: Mass spectrometry of human AD brain soluble Aβ aggregates. Fig.3 Human AD brain soluble Aβ aggregates mass spectrometry.4, 5

The specific method selected depends on the purpose of the experiment, the type of sample, and the resolution required. A combination of methods can provide a more comprehensive understanding of the mechanism of Aβ aggregation and its role in neurodegenerative diseases. Our services have helped many scientific research institutions and pharmaceutical companies achieve significant research results. Please contact us and we will match you with the most suitable Ph.D. scientist to communicate with you about your research and accelerate your plan.

References

  1. Polanco, David, et al. "Characterisation of Amyloid Aggregation and Inhibition by Diffusion-Based Single-Molecule Fluorescence Techniques." Biophysica 2.4 (2022): 506-524.
  2. Xue, Christine, et al. "Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation." Royal Society open science 4.1 (2017): 160696.
  3. Sehlin, Dag, et al. "Large aggregates are the major soluble Aβ species in AD brain fractionated with density gradient ultracentrifugation." PloS one 7.2 (2012): e32014.
  4. Esparza, Thomas J., et al. "Soluble amyloid-beta aggregates from human Alzheimer's disease brains." Scientific reports 6.1 (2016): 38187.
  5. Distributed under Open Access license CC BY 4.0, without modification.
For Research Use Only. Not For Clinical Use.
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