DESCRIPTION

Amino Acid Sequence

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val

General description

Amyloid β Protein Fragment 1-40 (Aβ40) is derived from the amyloid-β protein (Aβ), which is mapped to human chromosome 21q21.3. Aβ40 is predominantly present in the vascular amyloid deposits. Aβ40 comprises of C-terminal membrane insertion domain. It shows structural transition from random coil to a α-helical structure in a water-micelle medium.

Application

Amyloid β Protein Fragment 1-40 has been used:

  • in the temperature based conformational studies using Fourier transform infrared/differential scanning calorimetry (FT-IR/DSC) studies
  • as a reference standard in sandwich-type enzyme immunoassay for quantifying amyloid A4 protein in cerebrospinal fluid of patients with head trauma
  • as a component of embryonic stem cell medium to inhibit amyloid deposition in fibroblasts

Biochem/physiol Actions

Amyloid β-protein is neurotrophic and neurotoxic in vivo and in vitro in human and rat neuronal cell cultures. β-Amyloid peptides (amino acids 1-42 and 1-43) are the major constituents of senile plaques and neurofibrillary tangles that occur in the hippocampus, neocortex, and amygdala of patients with Alzheimer′s disease.
Amyloid β Protein Fragment 1-40 (Aβ40) forms cation based ion channels.

Reconstitution

For maximal biological activity, dilute the stock in calcium-free PBS to 1 mg/ml and incubate at 37 °C for 4 days.

Other Notes

Lyophilized from 0.1% TFA in H2O
amyloid

amyloid

Abstract

Alzheimer’s disease (AD) pathogenesis is widely believed to be driven by the production and deposition of the β-amyloid peptide (Aβ). For many years, investigators have been puzzled by the weak to nonexistent correlation between the amount of neuritic plaque pathology in the human brain and the degree of clinical dementia. Recent advances in our understanding of the development of amyloid pathology have helped solve this mystery. Substantial evidence now indicates that the solubility of Aβ, and the quantity of Aβ in different pools, may be more closely related to disease state. The composition of these pools of Aβ reflects different populations of amyloid deposits, and has definite correlates with the clinical status of the patient. Imaging technologies, including new amyloid imaging agents based on the chemical structure of histologic dyes, are now making it possible to track amyloid pathology along with disease progression in the living patient. Interestingly, these approaches indicate that the Aβ deposited in AD is different from that found in animal models. In general, deposited Aβ is more easily cleared from the brain in animal models, and does not show the same physical and biochemical characteristics as the amyloid found in AD. This raises important issues regarding the development and testing of future therapeutic agents.

Keywords: Amyloid, β-Amyloid Precursor Protein, Aβ, oligomer, fibril

 

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