The Role of Anionic Peptide Fragments in 1N4R Human Tau Protein Aggregation

Author(s): Mohammad Ali Nasiri Khalili, Gholamhossein Riazi, Shahin Ahmadian, Reza Khodarahmi, Sirus Khodadadi, Ali Afrasiabi, Oveis Karima, Farzad Mokhtari, Elham Hoveizi

Journal Name: Protein & Peptide Letters

Volume 21 , Issue 6 , 2014

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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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Article Details

Year: 2014
Published on: 23 December, 2013
Page: [511 - 516]
Pages: 6
DOI: 10.2174/0929866521666131223120713
Price: $65

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