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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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Impact of Amidation on Aβ25-35 Aggregation.

Judith C E Etaka1,2, Yan Lu1,2, Wei Kang2

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Amidation of amyloid-beta (Aβ) peptide fragments affects chain arrangement and secondary structure but not neurotoxicity. Glycine-rich motifs, not overall structure, appear key to Alzheimer's disease peptide toxicity.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Computational Biology

Background:

  • Toxic oligomeric species of amyloid-beta (Aβ) peptides are implicated in Alzheimer's disease pathogenesis.
  • The Aβ25-35 fragment retains the neurotoxicity of full-length Aβ42 and serves as a model for studying aggregation.

Purpose of the Study:

  • To investigate the impact of C-terminal amidation on the aggregation and structural properties of Aβ25-35 trimers using molecular dynamics simulations.
  • To determine the relationship between structural changes, fibrillation, and neurotoxicity in amidated versus nonamidated Aβ25-35.

Main Methods:

  • Molecular dynamics simulations of Aβ25-35 trimers in both amidated and nonamidated forms.
  • Analysis of aggregation pathways, secondary structure content (helix, β-sheet), and inter-chain contacts.

Main Results:

  • Amidation of Aβ25-35 resulted in a shift from antiparallel to parallel chain arrangements and increased helical content at the expense of β-sheets.
  • Despite structural differences, chain-chain contacts in both amidated and nonamidated systems were primarily mediated by Glycine (GxxxG) motifs and Isoleucine residues.
  • Neurotoxicity remained unchanged upon amidation, suggesting it is independent of these observed structural variations.

Conclusions:

  • The study implies that the aggregation-promoting Glycine motif is a more significant contributor to Aβ25-35 neurotoxicity than secondary or quaternary structures.
  • These findings suggest that targeting specific motifs, rather than overall structural conformations, may be a more effective strategy for mitigating Alzheimer's disease-related peptide toxicity.