Nickel(II) and Zinc(II) Binding to Tau Protein Fragments Containing Histidine and Cysteine
Faareha Mazhar, Noémi Piskolti, Viktória Kovács, Katalin Várnagy · 2026
Read Nickel(II) and Zinc(II) Binding to Tau Protein Fragments Containing Histidine and Cysteine by Faareha Mazhar, Noémi Piskolti, Viktória Kovács, Katalin Várnagy (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13437714.txt.
Description
Faareha Mazhar and colleagues measured how nickel and zinc ions grip fragments of tau, a protein that steadies nerve cell scaffolding and clumps in Alzheimer's disease. Metals may help drive that clumping, and tau's histidine and cysteine sites are likely handholds. Their 2026 study built five short tau pieces, some with one grip site, one a mutant, and one with both, then tracked binding with acidity measures and light spectroscopy.
Nickel took different holds by piece, favoring the cysteine sulfur in the combined fragment. Zinc's grip on that same two-site fragment grew much stronger than on single-site pieces, since the peptide could wrap the ion with two anchors. Such details matter: the form a metal takes at body acidity shapes whether it stays harmless or seeds aggregation. They stop at chemistry: no cells or animals were tested, so the step from binding to brain harm remains to be shown.
Catalog record
| CREATOR | Faareha Mazhar, Noémi Piskolti, Viktória Kovács, Katalin Várnagy |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 45889 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |