The role of anionic peptide fragments in 1N4R human tau protein aggregation

Protein Pept Lett. 2014 Jun;21(6):511-6. doi: 10.2174/0929866521666131223120713.


Cellular protein degradation systems are necessary to avoid the accumulation of misfolded or damaged proteins. Deficiency in these systems might cause to partial degradation of misfolded proteins and generation of amyloidogenic fragments. Protein misfolding is believed to be the primary cause of neurodegenerative disorders such as Alzheimer's disease (AD). In this study, we investigate effect of two anionic peptide fragments including, an acidic fragment of human Aβ (Aβ1-11) and a phosphorylated fragment of β-Casein (Tetraphosphopeptide), on tau protein aggregation. According to our results, these peptide fragments, induced tau fibrillization in vitro. In sum, we suggest that structural and conformational characters of inducer are as important as charge distribution on anionic inducer molecules however more experiments would be need to exactly confirm this suggestion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry
  • Amyloid beta-Peptides / metabolism*
  • Anions / chemistry
  • Anions / metabolism
  • Caseins / chemistry
  • Caseins / metabolism*
  • Humans
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism*
  • Phosphorylation
  • Protein Aggregation, Pathological / metabolism*
  • Protein Conformation
  • Protein Folding
  • tau Proteins / chemistry
  • tau Proteins / metabolism*


  • Amyloid beta-Peptides
  • Anions
  • Caseins
  • Peptide Fragments
  • amyloid beta-protein (1-12)
  • tau Proteins