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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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  11. Distinctive Contribution Of Two Additional Residues In Protein Aggregation Of Aβ42 And Aβ40 Isoforms.
  1. Home
  3. Research Domains
  5. Biological Sciences
  7. Industrial Biotechnology
  9. Bioprocessing, Bioproduction And Bioproducts
  11. Distinctive Contribution Of Two Additional Residues In Protein Aggregation Of Aβ42 And Aβ40 Isoforms.

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

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Distinctive contribution of two additional residues in protein aggregation of Aβ42 and Aβ40 isoforms.

Dongjoon Im1, Tae Su Choi1

  • 1Department of Life Sciences, Korea University, Seoul 02841, Korea.

BMB Reports
|June 5, 2024

View abstract on PubMed

Summary
This summary is machine-generated.

Amyloid-β (Aβ) aggregation, particularly the Aβ42 and Aβ40 isoforms, is central to Alzheimer's disease (AD) pathogenesis. Understanding the molecular differences driving Aβ42 aggregation is key for developing AD diagnostics and therapies.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Amyloid-β (Aβ) proteins, intrinsically disordered proteins (IDPs), self-assemble into aggregates, causing cell dysfunction and cytotoxicity.
  • While Aβ has beneficial roles, its hydrophobic nature promotes pathological aggregation linked to Alzheimer's disease (AD).
  • Aβ isoforms, like Aβ 1-42 (Aβ42) and Aβ 1-40 (Aβ40), are produced from amyloid-β precursor protein (APP) cleavage and are crucial in AD.

Purpose of the Study:

  • To elucidate the molecular mechanisms differentiating Aβ42 and Aβ40 amyloid aggregation.
  • To review the current understanding of Aβ42 and Aβ40 roles in AD progression.
  • To discuss the impact of heterogeneous Aβ isoform distribution on aggregation.

Main Methods:

  • Focus on the structural and mechanistic differences in amyloid aggregation between Aβ42 and Aβ40.
  • Analysis of the role of the two additional residues (Ile41 and Ala42) in Aβ42 aggregation.
  • Examination of aggregation in systems mimicking human cerebrospinal fluid (CSF) and plasma.

    • Main Results:

    • Aβ42's two extra residues significantly influence its aggregation mechanism compared to Aβ40.
    • Distinct structural features of Aβ42/Aβ40 amyloid fibrils are identified.
    • Heterogeneous Aβ distribution impacts aggregation dynamics.

    Conclusions:

    • The differential aggregation mechanisms of Aβ42 and Aβ40 are critical for AD pathogenesis.
    • Further research into these mechanisms can inform AD diagnosis and therapeutic strategies.
    • Understanding in vivo Aβ aggregation requires considering the interplay of different isoforms.