NDLI: Selective Inhibition of Aggregation and Toxicity of a Tau-Derived Peptide using Its Glycosylated Analogues

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Selective Inhibition of Aggregation and Toxicity of a Tau-Derived Peptide using Its Glycosylated Analogues

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Belostozky, Anna Abu-mokh, Amjaad Gazit, Ehud Segal, Daniel Richman, Michal Frenkel-pinter, Moran Rahimipour, Shai
Description	Author Affiliation: Frenkel-Pinter M ( Department Molecular Microbiology and Biotechnology, and the Interdisciplinary Sagol School of Neurosciences, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv, 69978, Israel.); Richman M ( Department of Chemistry, Bar-Ilan University, Ramat-Gan, 5290002, Israel.); Belostozky A ( Department of Chemistry, Bar-Ilan University, Ramat-Gan, 5290002, Israel.); Abu-Mokh A ( Department Molecular Microbiology and Biotechnology, and the Interdisciplinary Sagol School of Neurosciences, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv, 69978, Israel.); Gazit E ( Department Molecular Microbiology and Biotechnology, and the Interdisciplinary Sagol School of Neurosciences, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv, 69978, Israel. dsegal@post.tau.ac.il.); Rahimipour S ( Department of Chemistry, Bar-Ilan University, Ramat-Gan, 5290002, Israel. rahimis@biu.ac.il.); Segal D ( Department Molecular Microbiology and Biotechnology, and the Interdisciplinary Sagol School of Neurosciences, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Tel Aviv, 69978, Israel. ehudg@post.tau.ac.il.)
Abstract	Protein glycosylation is a ubiquitous post-translational modification that regulates the folding and function of many proteins. Misfolding of protein monomers and their toxic aggregation are the hallmark of many prevalent diseases. Thus, understanding the role of glycans in protein aggregation is highly important and could contribute both to unraveling the pathology of protein misfolding diseases as well as providing a means for modifying their course for therapeutic purposes. Using β-O-linked glycosylated variants of the highly studied Tau-derived hexapeptide motif VQIVYK, which served as a simplified amyloid model, we demonstrate that amyloid formation and toxicity can be strongly attenuated by a glycan unit, depending on the nature of the glycan itself. Importantly, we show for the first time that not only do glycans hinder self-aggregation, but the glycosylated peptides are capable of inhibiting aggregation of the non-modified corresponding amyloid scaffold.
ISSN	09476539
e-ISSN	15213765
Journal	Chemistry - A European Journal
Issue Number	17
Volume Number	22
Language	English
Publisher	Wiley-VCH;ChemPubSoc Europe
Publisher Date	2016-04-18
Publisher Place	Germany
Access Restriction	Open
Subject Keyword	Amyloid Antagonists & Inhibitors Chemistry Oligopeptides Peptides Tau Proteins Amino Acid Sequence Metabolism Glycosylation Protein Processing, Post-Translational Protein Structure, Secondary
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Catalysis

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