Abstract:
:Fibrous proteins discolor on exposure to the UV component of sunlight. This effect is exacerbated in the presence of fluorescent whitening agents (FWAs), which are often applied to textiles to improve product brightness. Tryptophan photoproducts have been identified as significant contributors to protein photoyellowing; however, the role of non-tryptophan-derived chromophores is less clear. In this study bovine collagen, containing no tryptophan residues, was irradiated in the presence and absence of the stilbene-derived FWA, 4,4'-bis(2-sulfostyryl)biphenyl (DSBP) and photoproducts were identified using mass spectrometry. Photoyellowing was found to be dependent on the presence of the FWA, attributed to amplified generation of reactive oxygen species (ROS), particularly hydroxyl radicals and peroxynitrite. Four key proteinaceous photomodifications contributing directly to photoyellowing were located in irradiated collagen pretreated with DSBP, namely dopa, nitrophenylalanine, nitrotyrosine and nitrohistidine. This represents the first direct characterization of the three nitrated residues in the photoyellowing of an isolated fibrous protein, and implicates the ROS, peroxynitrite, as a key contributor to protein photoyellowing. Direct oxidative modification of the FWA itself was also observed. This study demonstrates that, even in the absence of tryptophan residues, significant photomodification of protein residues leading to chromophore formation occurs in the presence of an FWA.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Dyer JM,Clerens S,Cornellison CD,Murphy CJ,Maurdev G,Millington KRdoi
10.1111/j.1751-1097.2009.00614.xsubject
Has Abstractpub_date
2009-11-01 00:00:00pages
1314-21issue
6eissn
0031-8655issn
1751-1097pii
PHP614journal_volume
85pub_type
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