Dimerisation of N-acetyl-L-tyrosine ethyl ester and Aß peptides via formation of dityrosine

Ali, Feda E., Leung, Andrew, Cherny, Robert A., Mavros, Christine, Barnham, Kevin J., Separovic, Frances and Barrow, Colin J. 2006, Dimerisation of N-acetyl-L-tyrosine ethyl ester and Aß peptides via formation of dityrosine, Free radical research, vol. 40, no. 1, pp. 1-9.

Attached Files
Name Description MIMEType Size Downloads

Title Dimerisation of N-acetyl-L-tyrosine ethyl ester and Aß peptides via formation of dityrosine
Formatted title Dimerisation of N-acetyl-L-tyrosine ethyl ester and Aß peptides via formation of dityrosine
Author(s) Ali, Feda E.
Leung, Andrew
Cherny, Robert A.
Mavros, Christine
Barnham, Kevin J.
Separovic, Frances
Barrow, Colin J.
Journal name Free radical research
Volume number 40
Issue number 1
Start page 1
End page 9
Publisher Gordon and Breach
Place of publication [London, England]
Publication date 2006-01
ISSN 1071-5762
1029-2470
Keyword(s) Alzheimer's disease
amyloid β peptide
horseradish peroxidase
metal catalyzed oxidation
oxidative stress
dityrosine
Summary Alzheimer's disease (AD) is characterised by the formation of amyloid deposits composed primarily of the amyloid β-peptide (Aβ). This peptide has been shown to bind redox active metals ions such as copper and iron, leading to the production of reactive oxygen species (ROS) and formation of hydrogen peroxide (H2O2). The generation of H2O2 has been linked with Aβ neurotoxicity and neurodegeneration in AD. Because of the relative stability of a tyrosyl radical, the tyrosine residue (Tyr-10) is believed to be critical to the neurotoxicity of Aβ. This residue has also been shown to be important to Aβ aggregation and amyloid formation. It is possible that the formation of an Aβ tyrosyl radical leads to increased aggregation via the formation of dityrosine as an early aggregation step, which is supported by the identification of dityrosine in amyloid plaque. The role of dityrosine formation in Aβ aggregation and neurotoxicity is as yet undetermined, partly because there are no facile methods for the synthesis of Aβ dimers containing dityrosine. Here we report the use of horseradish peroxidase and H2O2 to dimerise N-acetyl-l-tyrosine ethyl ester and apply the optimised conditions for dityrosine formation to fully unprotected Aβ peptides. We also report a simple fluorescent plate reader method for monitoring Aβ dimerisation via dityrosine formation.
Language eng
Field of Research 050299 Environmental Science and Management not elsewhere classified
111799 Public Health and Health Services not elsewhere classified
Socio Economic Objective 970105 Expanding Knowledge in the Environmental Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2006, Taylor & Francis
Persistent URL http://hdl.handle.net/10536/DRO/DU:30019467

Document type: Journal Article
Collection: School of Life and Environmental Sciences
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 15 times in TR Web of Science
Scopus Citation Count Cited 14 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 377 Abstract Views, 0 File Downloads  -  Detailed Statistics
Created: Tue, 15 Sep 2009, 12:49:01 EST by Rachael Mackenzie

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.