N-Terminally Truncated Aβ Peptide Variants in Alzheimer’s Disease
2019 | book part. A publication with affiliation to the University of Göttingen.
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- Authors
- Wirths, Oliver ; Zampar, Silvia; Weggen, Sascha
- Abstract
- The accumulation and aggregation of amyloid-β (Aβ) peptides in the brain is believed to be the initial trigger in the molecular pathology of Alzheimer’s disease (AD). In addition to the widely studied full-length Aβ peptides (mainly Aβ1–40 and Aβ1–42), a variety of amino-terminally truncated (N-truncated) peptides, such as AβpE3-x and Aβ4-x, have been detected in high abundance in autopsy samples from sporadic and familial AD patients. N-truncated Aβ species adopt specific physicochemical properties resulting in a higher aggregation propensity and increased peptide stability, which likely account for their neurotoxic potential. The presence of N-truncated Aβ peptides in transgenic mouse models of AD and the selective overexpression of specific N-truncated variants in the murine brain have facilitated their investigation in relevant in vivo settings. In this chapter, we address the pathological relevance of N-truncated Aβ peptide species and summarize the current knowledge about the enzymatic activities that might be involved in their generation.
- Issue Date
- 2019
- Organization
- Universitätsmedizin Göttingen
- ISBN
- 978-0-646-80968-7
- Language
- English
- Sponsor
- Open-Access-Publikationsfonds 2019