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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

—

Návaznosti

N - Vyzkumna aktivita podporovana z neverejnych zdroju

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

JOURNAL OF BIOLOGICAL PHYSICS

ISSN

0092-0606

e-ISSN

—

Svazek periodika

44

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

"237–243"

Kód UT WoS článku

000441201500001

EID výsledku v databázi Scopus

2-s2.0-85046652384