The Role of Anionic Peptide Fragments in 1N4R Human Tau Protein Aggregation
Mohammad Ali Nasiri Khalili, Gholamhossein Riazi, Shahin Ahmadian, Reza Khodarahmi, Sirus Khodadadi, Ali Afrasiabi, Oveis Karima, Farzad Mokhtari and Elham Hoveizi
Affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
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.
Keywords: Aggregation, β-Casein Tetraphosphopeptide, Human Aβ1-11, Protein misfolding, Tau.
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