AI Article Synopsis
- Amyloid-beta (Aβ) peptides are important in Alzheimer's disease due to their ability to bind transition metals, particularly Cu(II).
- A study found that a specific N-truncated Aβ analogue can form a stable Ni(II) complex in a high-spin state at physiological pH, allowing it to interact with phosphates and nucleotides.
- As pH rises, a transition to a low-spin Ni(II) complex occurs, and this interaction can significantly alter the electrochemical signals, suggesting potential applications in biosensors and implications for nickel toxicity.
Article Abstract
Amyloid-beta (Aβ) peptides, potentially relevant in the pathology of Alzheimer's disease, possess distinctive coordination properties, enabling an effective binding of transition-metal ions, with a preference for Cu(II). In this work, we found that a N-truncated Aβ analogue bearing a His-2 motif, Aβ, forms a stable Ni(II) high-spin octahedral complex at a physiological pH of 7.4 with labile coordination sites and facilitates ternary interactions with phosphates and nucleotides. As the pH increased above 9, a spin transition from a high-spin to a low-spin square-planar Ni(II) complex was observed. Employing electrochemical techniques, we showed that interactions between the binary Ni(II)-Aβ complex and phosphate species result in significant changes in the Ni(II) oxidation signal. Thus, the Ni(II)-Aβ complex could potentially serve as a receptor in electrochemical biosensors for phosphate species. The obtained results could also be important for nickel toxicology.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8693174 | PMC |
| http://dx.doi.org/10.1021/acs.inorgchem.1c03285 | DOI Listing |
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