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

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

Volume: 21 Issue: 6

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

Affiliation:

Keywords: Aggregation, β-Casein Tetraphosphopeptide, Human Aβ_1-11, Protein misfolding, Tau.

Abstract: 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 (Aβ_1–11) 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.

Cite this article as:

Khalili Ali Nasiri Mohammad, Riazi Gholamhossein, Ahmadian Shahin, Khodarahmi Reza, Khodadadi Sirus, Afrasiabi Ali, Karima Oveis, Mokhtari Farzad and Hoveizi Elham, The Role of Anionic Peptide Fragments in 1N4R Human Tau Protein Aggregation, Protein & Peptide Letters 2014; 21 (6) . https://dx.doi.org/10.2174/0929866521666131223120713