Photoexcited riboflavin induces oxidative damage to human serum albumin

摘要: Abstract Photoexcited riboflavin induced damage of human serum albumin (HSA), a water soluble protein, resulting in the diminishment fluorescence from tryptophan residue. Because hardly photosensitized singlet oxygen generation and sodium azide, quencher, did not inhibit protein damage, electron transfer-mediated oxidation HSA was speculated. Fluorescence lifetime affected by HSA, suggesting that excited triplet state is responsible for through transfer. In addition, preventive effect xanthone derivatives, quenchers, on could be evaluated using this reaction system HSA.