Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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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 and Elham Hoveizi

Affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.

Keywords: Aggregation, β-Casein Tetraphosphopeptide, Human Aβ1-11, 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 (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.

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Article Details

VOLUME: 21
ISSUE: 6
Page: [511 - 516]
Pages: 6
DOI: 10.2174/0929866521666131223120713