Photosensitized damage of protein by fluorinated diethoxyphosphorus(V)porphyrin

DOI Web Site 被引用文献2件 参考文献25件
  • Kazutaka Hirakawa
    Department of Basic Engineering (Chemistry), Faculty of Engineering, Shizuoka University, Johoku 3-5-1, Naka-ku, Hamamatsu, Shizuoka 432-8561, Japan
  • Keito Azumi
    Department of Basic Engineering (Chemistry), Faculty of Engineering, Shizuoka University, Johoku 3-5-1, Naka-ku, Hamamatsu, Shizuoka 432-8561, Japan
  • Yoshinobu Nishimura
    Department of Chemistry, University of Tsukuba, Tennodai 1-1-1, Tsukuba, Ibaraki 305-8571, Japan
  • Tatsuo Arai
    Department of Chemistry, University of Tsukuba, Tennodai 1-1-1, Tsukuba, Ibaraki 305-8571, Japan
  • Yoshio Nosaka
    Department of Materials Science and Technology, Nagaoka University of Technology, Kamitomioka 1603-1, Nagaoka, Niigata 940-2188, Japan
  • Segetoshi Okazaki
    Medical Photonics Research Center, Hamamatsu University School of Medicine, Handayama 1-20-1, Higashi-ku, Hamamatsu, Shizuoka 431-3192, Japan

書誌事項

公開日
2013-01
資源種別
journal article
DOI
  • 10.1142/s1088424612501258
公開者
World Scientific Pub Co Pte Ltd

この論文をさがす

説明

<jats:p>The effect of the axial ligand fluorination of the water-soluble P(V)porphyrin complex on photosensitized protein damage was examined. The activity of singlet oxygen generation by diethoxyP(V) porphyrin was slightly improved by the fluorination of the ethoxy chains. Absorption spectrum measurements demonstrated the binding interaction between the P(V)porphyrins and human serum albumin, a water-soluble protein. Photo-irradiated P(V)porphyrins damaged the amino acid residue of human serum albumin, resulting in the decrease of the fluorescence intensity from the tryptophan residue of human serum albumin. A singlet oxygen quencher, sodium azide, could not completely inhibit the damage of human serum albumin, suggesting that the electron transfer mechanism contributes to protein damage as does singlet oxygen generation. The decrease of the fluorescence lifetime of P(V)porphyrin by human serum albumin supported the electron transfer mechanism. The estimated contributions of the electron transfer mechanism are 0.57 and 0.44 for the fluorinated and non-fluorinated P(V)porphyrins, respectively. The total quantum yield of the protein photo-oxidation was slightly enhanced by this axial fluorination.</jats:p>

収録刊行物

被引用文献 (2)*注記

もっと見る

参考文献 (25)*注記

もっと見る

関連プロジェクト

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ