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Updated: Jan 11, 2026

Abbiategrasso Brain Bank Protocol for Collecting, Processing and Characterizing Aging Brains
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Pathological and Functional Brain Amyloids: A New Concept Explaining the Differences.

Alexey P Galkin1,2, Vladimir A Mitkevich3, Alexander A Makarov3

  • 1St. Petersburg Branch, Vavilov Institute of General Genetics, Russian Academy of Sciences, 199034 St. Petersburg, Russia.

International Journal of Molecular Sciences
|November 13, 2025
PubMed
Summary
This summary is machine-generated.

Brain amyloid proteins are not inherently toxic based on their composition. Instead, their toxicity depends on interactions with specific cellular targets, distinguishing harmful from functional amyloids.

Keywords:
amyloidogenic coresamyloids’ functional partnersbraincellular localizationcomparative analysisfunctional vs. pathological amyloidsneurodegenerative diseasesneurotoxicitypathological targetsprotein misfolding

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Amyloid proteins in the brain can be either functional or neurotoxic.
  • The reasons behind the differing effects of brain amyloids remain unclear.
  • Previous assumptions suggested amino acid composition dictates amyloid toxicity.

Purpose of the Study:

  • To compare the amino acid composition of pathological and functional brain amyloids.
  • To investigate the factors determining amyloid neurotoxicity.
  • To explore the concept of "available targets" in amyloid pathogenesis.

Main Methods:

  • Comparative analysis of amino acid sequences of brain amyloid proteins.
  • Review of existing evidence on amyloid interactions with cellular targets.
  • Examination of factors influencing target accessibility for functional amyloids.

Main Results:

  • Pathological and functional brain amyloids, and their fragments, show no significant differences in amino acid composition.
  • Amyloid toxicity is not solely due to amino acid sequence but influenced by interactions with specific targets.
  • Functional amyloids are protected from toxic interactions due to cellular localization or physiological binding.

Conclusions:

  • Amino acid composition does not differentiate toxic from non-toxic brain amyloids.
  • Amyloid toxicity arises from aberrant interactions with accessible cellular targets.
  • Functional amyloids avoid toxicity through compartmentalization or physiological interactions, rendering targets inaccessible.