ArticleChemistry (Weinheim an der Bergstrasse, Germany)2016
Solid-Phase Synthesis and Characterization of N-Terminally Elongated Aβ-3-x -Peptides.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Aggregation-Dependent Epitope Sequence and Modification Fingerprints of Anti-Aβ Antibodies.bioRxiv : the preprint server for biology · 2025Article
- Plasma amyloid-β precursor proteinThe journal of prevention of Alzheimer's disease · 2025Article
- ADAMTS4 is involved in the production of the Alzheimer disease amyloid biomarker APP669-711.Molecular psychiatry · 2023Article
- Is plasma amyloid-β 1-42/1-40 a better biomarker for Alzheimer's disease than AβX-42/X-40?Fluids and barriers of the CNS · 2022Article
- N-terminal heterogeneity of parenchymal and vascular amyloid-β deposits in Alzheimer's disease.Neuropathology and applied neurobiology · 2020Article
- Development and Technical Validation of an Immunoassay for the Detection of APPInternational journal of molecular sciences · 2020Article
- Reorientational Dynamics of Amyloid-β from NMR Spin Relaxation and Molecular Simulation.The journal of physical chemistry letters · 2019Article
- Modeling Amyloid-β42 Toxicity and Neurodegeneration in Adult Zebrafish Brain.Journal of visualized experiments : JoVE · 2017Article
- Solid-Phase Synthesis and Characterization of N-Terminally Elongated Aβ-3-x -Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2016Article
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8 authors.
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Abstract
In addition to the prototypic amyloid-β (Aβ) peptides Aβ1-40 and Aβ1-42 , several Aβ variants differing in their amino and carboxy termini have been described. Synthetic availability of an Aβ variant is often the key to study its role under physiological or pathological conditions. Herein, we report a protocol for the efficient solid-phase peptide synthesis of the N-terminally elongated Aβ-peptides Aβ-3-38 , Aβ-3-40 , and Aβ-3-42 . Biophysical characterization by NMR spectroscopy, CD spectroscopy, an aggregation assay, and electron microscopy revealed that all three peptides were prone to aggregation into amyloid fibrils. Immunoprecipitation, followed by mass spectrometry, indicated that Aβ-3-38 and Aβ-3-40 are generated by transfected cells even in the presence of a tripartite β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor. The elongated Aβ peptides starting at Val(-3) can be separated from N-terminally-truncated Aβ forms by high-resolution isoelectric-focusing techniques, despite virtually identical isoelectric points. The synthetic Aβ variants and the methods presented here are providing tools to advance our understanding of the potential roles of N-terminally elongated Aβ variants in Alzheimer's disease.
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