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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.

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Authors and Affiliations

  1. The Heart Research Institute, 7 Eliza Street, Newtown, Sydney, NSW, 2042, Australia

    David I. Pattison, Aldwin Suryo Rahmanto & Michael J. Davies

  2. Faculty of Medicine, University of Sydney, Sydney, NSW, 2006, Australia

    David I. Pattison & Michael J. Davies

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  1. David I. Pattison
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Contribution to the themed issue on the biology of UVA.

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Pattison, D.I., Rahmanto, A.S. & Davies, M.J. Photo-oxidation of proteins. Photochem Photobiol Sci 11, 38–53 (2012). https://doi.org/10.1039/c1pp05164d

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