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Issue 1, 2012
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Photo-oxidation of proteins

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Abstract

Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280–320 nm) and UVA radiation (λ 320–400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals. Indirect protein damage can occur via singlet oxygen (1O21Δg), with this resulting in damage to Trp, Tyr, His, cystine, cysteine (Cys) and methionine (Met) residues. Although initial damage is limited to these residues multiple secondary processes, that occur both during and after radiation exposure, can result in damage to other intra- and inter-molecular sites. Secondary damage can arise via radicals (e.g. Trp, Tyr and Cys radicals), from reactive intermediates generated by 1O2 (e.g. Trp, Tyr and His peroxides) and via molecular reactions of photo-products (e.g. reactive carbonyls). These processes can result in protein fragmentation, aggregation, altered physical and chemical properties (e.g. hydrophobicity and charge) and modulated biological turnover. Accumulating evidence implicates these events in cellular and tissue dysfunction (e.g.apoptosis, necrosis and altered cell signaling), and multiple human pathologies.

Graphical abstract: Photo-oxidation of proteins

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Publication details

The article was received on 01 Jun 2011, accepted on 14 Jul 2011 and first published on 22 Aug 2011


Article type: Perspective
DOI: 10.1039/C1PP05164D
Citation: Photochem. Photobiol. Sci., 2012,11, 38-53
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    Photo-oxidation of proteins

    D. I. Pattison, A. S. Rahmanto and M. J. Davies, Photochem. Photobiol. Sci., 2012, 11, 38
    DOI: 10.1039/C1PP05164D

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