Heme Binding Induces Dimerization and Nitration of Truncated β‐Amyloid Peptide Aβ16 Under Oxidative Stress
Identifieur interne : 000E75 ( Main/Exploration ); précédent : 000E74; suivant : 000E76Heme Binding Induces Dimerization and Nitration of Truncated β‐Amyloid Peptide Aβ16 Under Oxidative Stress
Auteurs : F. Thiabaud [Italie] ; F. Pizzocaro [Italie] ; F. Garcia-Serres [France] ; F. Latour [France] ; F. Monzani [Italie] ; F. Casella [Italie]Source :
- Angewandte Chemie [ 0044-8249 ] ; 2013-07-29.
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Abstract
Stressige Situation: Bei der Bindung von FeIII‐Häm an Aβ16 entsteht ein Gleichgewicht aus fünffach koordiniertem [Hämin(Aβ16)] und sechsfach koordiniertem [Hämin(Aβ16)2], das vom Aβ16/Hämin‐Verhältnis und der Temperatur abhängt. Unter oxidativem und nitrosativem Stress vermitteln die Häm‐Aβ16‐Komplexe Peroxidase‐artige Reaktionen, welche die Oxidation und Nitrierung des Tyr10‐Restes von Aβ verursachen. Sowohl Dityrosinbildung als auch Tyrosin‐Nitrierung verstärken die Aβ‐Aggregation.
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DOI: 10.1002/ange.201302989
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Unter oxidativem und nitrosativem Stress vermitteln die Häm‐Aβ16‐Komplexe Peroxidase‐artige Reaktionen, welche die Oxidation und Nitrierung des Tyr10‐Restes von Aβ verursachen. Sowohl Dityrosinbildung als auch Tyrosin‐Nitrierung verstärken die Aβ‐Aggregation.</div></front></TEI><affiliations><list><country><li>France</li><li>Italie</li></country></list><tree><country name="Italie"><noRegion><name sortKey="Thiabaud, F" sort="Thiabaud, F" uniqKey="Thiabaud F" first="F." last="Thiabaud">F. Thiabaud</name></noRegion><name sortKey="Casella, F" sort="Casella, F" uniqKey="Casella F" first="F." last="Casella">F. Casella</name><name sortKey="Casella, F" sort="Casella, F" uniqKey="Casella F" first="F." last="Casella">F. Casella</name><name sortKey="Monzani, F" sort="Monzani, F" uniqKey="Monzani F" first="F." last="Monzani">F. Monzani</name><name sortKey="Pizzocaro, F" sort="Pizzocaro, F" uniqKey="Pizzocaro F" first="F." last="Pizzocaro">F. 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