Journal article

Characterization and Identification of Dityrosine Cross-Linked Peptides Using Tandem Mass Spectrometry

Soumya Mukherjee, Eugene A Kapp, Amber Lothian, Anne M Roberts, Yury V Vasil'ev, Berin A Boughton, Kevin J Barnham, W Mei Kok, Craig A Hutton, Colin L Masters, Ashley I Bush, Joseph S Beckmann, Somdatta Ghosh Dey, Blaine R Roberts

ANALYTICAL CHEMISTRY | AMER CHEMICAL SOC | Published : 2017

Abstract

The use of mass spectrometry coupled with chemical cross-linking of proteins has become a powerful tool for proteins structure and interactions studies. Unlike structural analysis of proteins using chemical reagents specific for lysine or cysteine residues, identification of gas-phase fragmentation patterns of endogenous dityrosine cross-linked peptides have not been investigated. Dityrosine cross-linking in proteins and peptides are clinical markers of oxidative stress, aging, and neurodegenerative diseases including Alzheimer's disease and Parkinson's disease. In this study, we investigated and characterized the fragmentation pattern of a synthetically prepared dityrosine cross-linked dime..

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Grants

Funding Acknowledgements

Supported by the Cooperative Research Centre (CRC) for Mental Health, an Australian Government initiative, the Australian Research Council Linkage Projects Scheme (with Agilent Technologies), and the Victorian Government Operational Infrastructure Support Program. S.M. is the recipient of Institute Senior Research Fellowship at IACS, Kolkata. We thank Professor Roberto Cappai for the gift of the a-synuclein plasmid used for recombinant proteins expression and Liping Yang and Claudia Maier for the use of the Lumos Orbitrap in the OSU Biomolecular Mass Spectrometry Core Facility. We thank the Mass Spectrometry and Proteomics Facility at Bio21 Institute, Melbourne, and the Neuroproteomics Facility at the Florey Institute.