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Beta-Amyloid (1-16), sequence DAEFRHDSGYEVHHQK, is the N-terminal metal-binding domain of human amyloid-β peptide. This fragment contains key residues involved in coordination of transition metal ions, including histidine residues His6, His13, and His14, as well as additional donor groups that contribute to copper and zinc binding.
Unlike full-length Aβ (1-40) or Aβ (1-42), Aβ (1-16) is commonly used as a soluble model peptide for studying metal coordination, redox chemistry, and the early molecular events associated with Alzheimer’s disease-related amyloid biology. It allows researchers to focus specifically on the N-terminal metal-binding region without the strong hydrophobic aggregation behavior of the C-terminal domain.
Research Background
The N-terminal region of amyloid-β plays an important role in binding metal ions such as Cu(II), Cu(I), Zn(II), and Fe(III). Metal binding to Aβ has been linked to peptide aggregation, oxidative stress, and reactive oxygen species generation in Alzheimer’s disease research. Aβ (1-16) is therefore widely used in biochemical and biophysical studies that examine how metal coordination affects peptide structure and reactivity.
Published studies have shown that copper binding to Aβ (1-16) is pH-dependent and can involve nitrogen and oxygen donor atoms within the peptide. Histidine residues are central to metal coordination, while Tyr10 and other N-terminal residues may also contribute depending on oxidation state and experimental conditions.
Applications in Alzheimer’s Disease Research
- Metal-binding studies of amyloid-β
- Copper and zinc coordination analysis
- Redox chemistry and oxidative stress research
- Reactive oxygen species generation assays
- NMR, EPR, CD, UV-visible, and mass spectrometry studies
- Comparison with full-length Aβ (1-40) and Aβ (1-42)
Metal Coordination and Biophysical Studies
Aβ (1-16) is especially useful for studying Cu(II), Cu(I), and Zn(II) binding because it contains the primary metal-binding region of the full-length amyloid-β peptide. Researchers use this fragment to characterize binding affinity, ligand coordination geometry, pH effects, and competition between different metal ions.
This peptide is also valuable in studies examining how metal ions influence Aβ structure and aggregation pathways. Zinc binding to the N-terminal domain has been associated with amyloid assembly, while copper-bound Aβ species are frequently investigated for their redox activity and potential contribution to oxidative damage.
Why Use Aβ (1-16)?
- Contains the key N-terminal metal-binding domain of amyloid-β
- Less aggregation-prone than full-length Aβ peptides
- Useful for copper, zinc, and iron coordination studies
- Compatible with high-resolution spectroscopic analysis
- Important model peptide for Alzheimer’s disease metal homeostasis research
Related Products and Resources
Beta-Amyloid (1-42), human
Beta-Amyloid (1-40), Ultra Pure, TFA
Amyloid peptide category
Amyloid Peptides for Alzheimer’s Disease Research
Research Use Only. Not for human or therapeutic use.
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