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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
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Aβ42 and Aβ40: similarities and differences.

Tian Qiu1, Qian Liu1, Yong-Xiang Chen1

  • 1Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing, 100084, China.

Journal of Peptide Science : an Official Publication of the European Peptide Society
|May 29, 2015
PubMed
Summary
This summary is machine-generated.

Alzheimer's disease is linked to amyloid-β (Aβ) peptide buildup. This review compares Aβ40 and Aβ42, crucial Aβ forms, highlighting their distinct properties and potential therapeutic targets.

Keywords:
Aβ oligomersAβ40Aβ42aggregation mechanismamyloid-β peptide

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Alzheimer's disease (AD) is characterized by the abnormal accumulation of amyloid-beta (Aβ) peptides in the brain.
  • Aβ peptides are derived from the amyloid precursor protein (APP) through proteolytic cleavage.
  • The amyloid hypothesis posits that Aβ accumulation drives AD pathogenesis.

Purpose of the Study:

  • To review and compare the similarities and differences between Aβ40 and Aβ42 isoforms.
  • To discuss the distinct metabolism, physiological functions, toxicities, and aggregation mechanisms of Aβ40 and Aβ42.
  • To highlight recent advancements in selective inhibitors and probes targeting these Aβ isoforms.

Main Methods:

  • Literature review and synthesis of existing research on Aβ peptides.
  • Comparative analysis of biochemical and functional properties of Aβ40 and Aβ42.
  • Summary of studies on therapeutic strategies and diagnostic tools.

Main Results:

  • Aβ40 and Aβ42, despite differing by only two amino acids, exhibit significant variations.
  • These variations impact their aggregation propensity, toxicity, and roles in AD.
  • Selective inhibitors and probes are being developed to target specific Aβ isoforms.

Conclusions:

  • Understanding the differential characteristics of Aβ40 and Aβ42 is critical for AD research.
  • Targeting specific Aβ isoforms offers a promising therapeutic avenue.
  • Further research into selective inhibitors and probes is essential for developing effective AD treatments.