Stereospecific interactions of amyloid ß peptides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12110%2F10%3A00012125" target="_blank" >RIV/60076658:12110/10:00012125 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00023752:_____/10:00001107

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Stereospecific interactions of amyloid ß peptides

Popis výsledku v původním jazyce

Although causes of Alzheimer disease are not known yet in a detail, it appears that amyloid ß peptides can play a key role in the pathogenesis of the dementia. The toxicity of peptides is closely associated with their ability to oligomerize and aggregateor to create complexes with various endogenous molecules (e.g., with receptors, carriers, enzymes, oxysterols, etc.). However, mechanisms of their physiological interactions and the shift to pathological effects have not been yet cleared up. The experimental results indicate that the physiological actions of peptides are probably associated with the monomeric soluble L-isoform and mediated by stereospecific binding to corresponding molecule. Synthetic D-isoforms or reverse peptides are not effective here. On the other hand, the toxic actions of aggregated L- and D-isoforms on membranes are very similar. In the study, the complexes of amyloid ß peptides and of R-/S-oxysterols are compared. Possible applications of naturally occurring en

Název v anglickém jazyce

Stereospecific interactions of amyloid ß peptides

Popis výsledku anglicky

Although causes of Alzheimer disease are not known yet in a detail, it appears that amyloid ß peptides can play a key role in the pathogenesis of the dementia. The toxicity of peptides is closely associated with their ability to oligomerize and aggregateor to create complexes with various endogenous molecules (e.g., with receptors, carriers, enzymes, oxysterols, etc.). However, mechanisms of their physiological interactions and the shift to pathological effects have not been yet cleared up. The experimental results indicate that the physiological actions of peptides are probably associated with the monomeric soluble L-isoform and mediated by stereospecific binding to corresponding molecule. Synthetic D-isoforms or reverse peptides are not effective here. On the other hand, the toxic actions of aggregated L- and D-isoforms on membranes are very similar. In the study, the complexes of amyloid ß peptides and of R-/S-oxysterols are compared. Possible applications of naturally occurring en

Druh

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

CEP obor

FH - Neurologie, neurochirurgie, neurovědy

OECD FORD obor

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Projekt

<a href="/cs/project/GA305%2F09%2F0457" target="_blank" >GA305/09/0457: Testování vazby mezi cerebrosterolem a peptidem amyloidu beta 1-40</a><br>

Návaznosti

V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

Psychiatrie

ISSN

1211-7579

e-ISSN

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Svazek periodika

14

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

4

Strana od-do

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Kód UT WoS článku

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EID výsledku v databázi Scopus

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