Heme Binding Induces Dimerization and Nitration of Truncated β‐Amyloid Peptide Aβ16 Under Oxidative Stress1. Issue 31 (20th June 2013)

• Record Type: Journal Article
• Authors: Thiabaud, Grégory; Pizzocaro, Silvia; Garcia‐Serres, Ricardo; Latour, Jean‐Marc; Monzani, Enrico; Casella, Luigi
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 31(2013)
• Page Start: 8041
• Page End: 8044
• Publication Date: 2013-06-20
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201302989
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Stressful situation</bold>: Ferric heme binds to Aβ16 giving a mixture of five‐coordinate [hemin(Aβ16)] and six‐coordinate [hemin(Aβ16)₂] species, the equilibrium of which depends on the Aβ16/hemin ratio and on temperature. Under oxidative and nitrative stress conditions the heme–Aβ16 complexes promote peroxidase‐like reactions causing oxidation and nitration of the Aβ Tyr10 residue. Both dityrosine formation and tyrosine nitration strongly enhance Aβ aggregation.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg276x48t7" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>