β-Amyloid (HFIP-treated) and Salts (HCI,TFA)
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β-Amyloid (HFIP-treated) and Salts (HCI,TFA)

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CAD-002 Amyloid β-Protein (1-42) hydrochloride salt Inquiry
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Introduction

Alzheimer’s disease (AD) is a neurodegenerative disease and the pathogenesis is still unclear. β -amyloid (Aβ) is one of the specific biomarkers of AD. Numerous clinical studies have suggested that abnormal levels of Aβ in blood, cerebrospinal fluid and brain tissue are closely related to the progression of AD. Hexafluoroisopropanol, commonly abbreviated as HFIP, is an organic compound having the formula (CF3)2CHOH. The fluorinated alcohol can be used as a solvent and a synthetic intermediate. It looks like a colorless, volatile liquid with a strong pungent odor. As a solvent, hexafluoro-2-propanol is polar and exhibits strong hydrogen bonding properties, enabling it to dissolve substances as hydrogen bond acceptors, such as amides and ethers. Hexafluoro-2-propanol is transparent to UV light and has high density, low viscosity and low refractive index. Hexafluoroisopropanol as a good solvent for β -amyloid (Aβ). The analysis and evaluation of Aβ is of great significance for the early detection, tracking, prevention and treatment of AD.

Mechanism of action

Alzheimer’s disease is characterized by the presence of cerebral amyloid plaques deposited around nerve cells that eventually erode and destroy normal brain processes. The main protein component of this plaque is the isoform (Aβ) of β-amyloid with a 39-43 residue in a coacervated form. The main cause of senile dementia is the formation of the fibrous amyloid plaques in the brain parenchyma and vasculature. Aβ is formed following sequential cleavage of amyloid precursor protein (APP), an undetermined functional transmembrane glycoprotein. APP can be cleaved by proteolytic enzymes α-, β- and γ-secretase. Aβ protein is produced by the continuous action of β and γ secretase.

Application of β-Amyloid (HFIP-treated) and Salts

The normal function of Aβ is unclear. Although some animal studies have shown that the loss of Aβ does not result in any significant loss of physiological function, several potential activities of Aβ have been discovered, including activation of kinases, against oxidative stress, regulate cholesterol transport, as a transcription factor, and antimicrobial activity (possibly related to the proinflammatory activity of Aβ).

References
1. Ashall, F., & Goate, A. M. (1994). Role of the β-amyloid precursor protein in Alzheimer's disease. Trends in biochemical sciences, 19(1), 42-46.
2. Volloch, V., & Rits, S. (2018). Results of beta secretase-inhibitor clinical trials support amyloid precursor protein-independent generation of beta amyloid in sporadic alzheimer’s disease. Medical Sciences, 6(2), 45.
3. Ubelmann, F., Burrinha, T., & Almeida, C. G. (2017). A Novel Protocol to Quantitatively Measure the Endocytic Trafficking of Amyloid Precursor Protein (APP) in Polarized Primary Neurons with Sub-cellular Resolution. EMBO Reports.

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