Fe(II) formation after interaction of the amyloid β-peptide with iron storage protein ferritin

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F18%3A73590888" target="_blank" >RIV/61989592:15310/18:73590888 - isvavai.cz</a>
Result on the web
<a href="https://link.springer.com/article/10.1007%2Fs10867-018-9498-3" target="_blank" >https://link.springer.com/article/10.1007%2Fs10867-018-9498-3</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s10867-018-9498-3" target="_blank" >10.1007/s10867-018-9498-3</a>

Result language
angličtina
Original language name
Fe(II) formation after interaction of the amyloid β-peptide with iron storage protein ferritin
Original language description
The interaction of amyloid β-peptide (Aβ) with the iron-storage protein ferritin was studied in vitro. We have shown that Aβ during fibril formation process is able to reduce Fe(III) from the ferritin core (ferrihydrite) to Fe(II). The Aβ-mediated Fe(III) reduction yielded a two-times-higher concentration of free Fe(II) than the spontaneous formation of Fe(II) by the ferritin itself. We suggest that Aβ can also act as a ferritin-specific metallochaperone-like molecule capturing Fe(III) from the ferritin ferrihydrite core. Our observation may partially explain the formation of Fe(II)-containing minerals in human brains suffering by neurodegenerative diseases.
Czech name
—
Czech description
—

Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10610 - Biophysics

Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)