Amyloid-beta Peptide Oligomerization Assay Service

Our services have enabled numerous researchers to successfully conduct studies on amyloid beta peptide (Aβ) oligomers in Alzheimer's disease (AD) and other neurodegenerative diseases. For more information on the products and services provided, project-specific consultations, and pricing, please submit an inquiry here.

Introduction

Isoforms of Aβ

Based on different amino acid sequences and structural characteristics, Aβ peptides can be divided into several isoforms, the most common of which are Aβ1-40 and Aβ1-42. The concentrations of these two subtypes in cerebrospinal fluid and blood differ significantly, with Aβ1-42 concentrations typically 10 times lower than Aβ1-40, but it is more toxic and more likely to form amyloid plaques, thereby causing neurotoxicity. An increase in the Aβ42 / Aβ40 ratio is associated with familial AD.

Amyloid-beta Peptide Oligomerization Assays

• Electrophoresis-based assay

Electrophoresis technology plays an important role in monitoring the Aβ aggregation process, particularly capillary electrophoresis (HPCE) and gel electrophoresis (SDS-PAGE), which can provide important information about the morphology, size and dynamics of aggregates. HPCE can rapidly separate Aβ monomers and aggregates, and when combined with laser-induced fluorescence detection (LIF) and other technologies, accurate analysis of different aggregation states can be achieved. SDS-PAGE can observe Aβ aggregates of different molecular weights, such as dimers, trimers and tetramers.

Fig.1 The mixture of Aβ40 and Aβ42 was analyzed by SDS-PAGE.^{2, 4}

• ELISA-based assay

Enzyme-linked immunosorbent assay (ELISA) is a commonly used method for detecting Aβ oligomers that can specifically identify and quantify different types of Aβ oligomers.

• Fluorescence-based assay

Using fluorescent labeling technology, researchers can monitor the self-assembly process of Aβ peptides in real time. For example, by binding fluorescent dyes to Aβ peptides, dynamic changes in oligomerization, lag and growth phases can be observed. This method helps to reveal the formation mechanism of Aβ oligomers and their effects on neurons.

• Custom assays

We offer the ability to customize Aβ peptide oligomerization assays to suit your specific needs. In addition, we provide high-quality materials, data, and insights to support the success of your projects. Please contact us to discuss your project plans and our expert scientists will be happy to assist with accelerating your research.

References

1. Rudajev, Vladimir, and Jiri Novotny. "The role of lipid environment in ganglioside GM1-induced amyloid β aggregation." Membranes 10.9 (2020): 226.
2. Pujol-Pina, Rosa, et al. "SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer s disease: appealing for ESI-IM-MS." Scientific reports 5.1 (2015): 14809.
3. Willbold, Dieter, et al. "Blood‐based quantification of Aβ oligomers indicates impaired clearance from brain in ApoE ε4 positive subjects." Alzheimer's & Dementia 19 (2023): e082922.
4. Distributed under Open Access license CC BY 4.0, without modification.