A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry : probing the pathogenesis of chronic disease

Zhang, Qibin, Ames, Jenny, Smith, Richard, Baynes, John and Metz, Thomas (2009) A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry : probing the pathogenesis of chronic disease. Journal of Proteome Research, 8 (2). pp. 754-769. ISSN 1535-3893

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Official URL: http://dx.doi.org/10.1021/pr800858h

Abstract

Formation of AGEs (advanced glycation end-products) and ALEs (advanced lipoxidation end-products) on proteins is associated with aging and various diseases of oxidative stress, notably diabetes and its complications. Modification of protein to AGE/ALEs is known to be site-directed and this has potential implications for protein functionality and design of AGE/ALE inhibitors. Determination of the site-specificity of modification is achieved most efficiently by MS. The present paper summarizes some of the challenges that need to be addressed when determining the site-specificity of AGE/ALE formation on protein by MS, using the protein RNase as an example. The following topics are discussed: formation and significance of AGE/ALEs, location of glycated peptides, enzymic digestion of glycated peptides and selection of mass spectrometric settings of analysis for glycated peptides.

Item Type: Article
Uncontrolled Keywords: advanced glycation end-products (AGEs), diabetes mellitus, mass spectrometry
Subjects: F100 Chemistry
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: EPrints Services
Date Deposited: 11 Feb 2010 14:17
Last Modified: 10 Aug 2015 11:45
URI: http://nrl.northumbria.ac.uk/id/eprint/1495

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