Unmodified and pyroglutamylated amyloid β peptides form hypertoxic hetero‐oligomers of unique secondary structure
نویسندگان
چکیده
منابع مشابه
Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid β peptides.
Amyloid β peptide (Aβ) is causatively associated with Alzheimer's disease (AD), and N-terminally truncated and pyroglutamylated Aβ peptides (AβpE) exert hypertoxic effect by an unknown mechanism. Recent evidence has identified the prefibrillar oligomers of Aβ, not the fibrils, as the prevalent cytotoxic species. Structural characterization of Aβ and AβpE oligomers is therefore important for bet...
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ژورنال
عنوان ژورنال: The FEBS Journal
سال: 2017
ISSN: 1742-464X,1742-4658
DOI: 10.1111/febs.14058