Toxic Amyloid-beta Peptide 1-42 Exposure Assay Service
In recent years, the emergence of more and more in vitro models has provided a broad prospect for Alzheimer's disease (AD) research. Intoxication of neurons by β-amyloid (Aβ1-42) oligomers is a promising in vitro model of AD for rapid screening of potential neuroprotective molecules. With our advanced technology and professional scientists, Creative Biolabs focuses on providing comprehensive Aβ1-42 induced neurotoxicity assay services for customers all over the world.
Relationship of AD and Aβ
AD is a common neurodegenerative disease. The main histopathological feature of AD is the presence of senile plaques (SP). The major component of SP is the Aβ, which is derived from the proteolytic cleavage of the amyloid precursor protein (APP). The accumulation of Aβ leads to the formation of Aβ fibrils observed in the brains of AD patients, and these abnormal structures alter the shape of neurons, leading to impaired communication between neurons.
Isoforms of Aβ
Monomeric Aβ peptides include various isoforms, including Aβ1-40, Aβ1-42, and Aβ1-43, as well as many N-terminally truncated isoforms. Aβ1-40 and Aβ1-42 make up most of the Aβ peptides found in the human brain. In the amyloidogenic pathway, the monomers of the Aβ1-40 and Aβ1-42 peptides are derived from APP and form aggregates of different molecular weights, resulting in amyloid plaques. It is worth noting that Aβ1-40 is soluble and less toxic, representing the most abundant form of Aβ in the brain. Compared to Aβ1-40, Aβ1-42 is highly neurotoxic and has two additional hydrophobic amino acids that promote more fibril formation in Ab42.
Fig.1 Aβ1-40 and Aβ1-42. (Cerofolini, et al., 2020)
Toxic Aβ1-42 Exposure Assay
It is well known that oxidative stress is closely related to AD. Aβ1-42 has been reported to induce oxidative stress and neurotoxicity both in vitro and in vivo. In addition, the biochemical analysis indicated that the main component of senile plaque amyloid was Aβ1-42, which increasingly accumulated in brain neurons thereby causing AD. Taken together, Aβ1-42 is considered to play a central role in the pathogenesis of AD as a mediator of oxidative stress. In our assay, AD cell models were constructed by treating specific cells with Aβ1-42. Creative Biolabs evaluated the neuroprotective effect of compounds against AD by the following methods.
- Quantitative real-time PCR (qPCR) assay
- CCK-8 assay
- Enzyme-linked immunosorbent assay (ELISA) assay
- Flow cytometry assay
Self-assembly of Aβ, especially Aβ1-42, into oligomers and fibrils is one of the major pathological events associated with AD. Aβ1-42 investigations provide broad prospects in AD drug development. Creative Biolabs is committed to providing specific in vitro models and multi-channel Aβ1-42 detection solutions to advance the research of nervous system drugs. If you have any questions about the toxic Aβ1−42 exposure assay, please contact us for more details.
Reference
- Cerofolini, L.; et al. Mixing Aβ (1–40) and Aβ (1–42) peptides generates unique amyloid fibrils. Chemical Communications. 2020, 56(62): 8830-8833.
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