Molecular dynamic studies of amyloid-beta interactions with curcumin and Cu2+ ions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00084946" target="_blank" >RIV/00216224:14740/15:00084946 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.degruyter.com/view/j/chempap.2015.69.issue-9/chempap-2015-0134/chempap-2015-0134.xml" target="_blank" >http://www.degruyter.com/view/j/chempap.2015.69.issue-9/chempap-2015-0134/chempap-2015-0134.xml</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1515/chempap-2015-0134" target="_blank" >10.1515/chempap-2015-0134</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Molecular dynamic studies of amyloid-beta interactions with curcumin and Cu2+ ions

Popis výsledku v původním jazyce

Amyloid-beta (A beta) peptide readily forms aggregates that are associated with Alzheimer's disease. Transition metals play a key role in this process. Recently, it has been shown that curcumin (CUA), a polyphenolic phytochemical, inhibits the aggregation of A beta peptide. However, interactions of A beta peptide with metal ions or CUA are not entirely clear. In this work, molecular dynamics (MD) simulations were carried out to clear the nature of interactions between the 42-residue A beta peptide (A beta-42) and Cu2+ ions and CUA. Altogether nine different models were investigated, and more than 2 mu s of the simulation data were analyzed. The models represent the possible modes of arrangement between A beta-42 and Cu2+ ions and CUA, respectively, andwere used to shed light on the A beta-42 conformational behavior in the presence of Cu2+ ions and CUA molecules.

Název v anglickém jazyce

Molecular dynamic studies of amyloid-beta interactions with curcumin and Cu2+ ions

Popis výsledku anglicky

Amyloid-beta (A beta) peptide readily forms aggregates that are associated with Alzheimer's disease. Transition metals play a key role in this process. Recently, it has been shown that curcumin (CUA), a polyphenolic phytochemical, inhibits the aggregation of A beta peptide. However, interactions of A beta peptide with metal ions or CUA are not entirely clear. In this work, molecular dynamics (MD) simulations were carried out to clear the nature of interactions between the 42-residue A beta peptide (A beta-42) and Cu2+ ions and CUA. Altogether nine different models were investigated, and more than 2 mu s of the simulation data were analyzed. The models represent the possible modes of arrangement between A beta-42 and Cu2+ ions and CUA, respectively, andwere used to shed light on the A beta-42 conformational behavior in the presence of Cu2+ ions and CUA molecules.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/ED1.1.00%2F02.0068" target="_blank" >ED1.1.00/02.0068: CEITEC - central european institute of technology</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Chemical papers

ISSN

0366-6352

e-ISSN

—

Svazek periodika

69

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

15

Strana od-do

1262-1276

Kód UT WoS článku

000355416200014

EID výsledku v databázi Scopus

—