Reductive modification of a methionine residue

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F06%3A00022544" target="_blank" >RIV/60461373:22330/06:00022544 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Reductive modification of a methionine residue

Original language description

The amyloid beta peptide suffers from the highly selective attack of H-radical atoms on the Met35 residue, with the formation of a modified peptide containing an a-aminobutyric acid residue. This chemical reactivity could represent the molecular basis ofa posttranslational modification of the amyloid beta peptide which could infer interesting biological effects. The formation of trans-lipids as a marker of radical damage to methionine-containing peptides was also evaluated. The system of 1-palmitoyl-2-oleoyl phosphatidylcholine vesicles containing amyloid beta peptide modeled the occurrence of radical damage that is transferred from the peptide to the lipid domain. This suggests a link between lipidomics and proteomics, due to the known interaction ofthe amyloid beta protein with cell membranes.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

S - Specificky vyzkum na vysokych skolach

Publication year

2006

Confidentiality

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

Name of the periodical

Angewandte Chemie-International Edition

ISSN

1433-7851

e-ISSN

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Volume of the periodical

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Issue of the periodical within the volume

16

Country of publishing house

DE - GERMANY

Number of pages

4

Pages from-to

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UT code for WoS article

000236815700025

EID of the result in the Scopus database

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