Superoxide Dismutase Activities of Ironporphyrins Modified with Poly (L-lysine)

Novel superoxide dismutase (SOD) mimics, the macromolecule-ironporphyrin possessing poly(L-lysine) (PLLN) and iron tetraphenylporphyrin derivative are synthesized and their SOD activities are evaluated. The synthesis of PLLN-bound iron nicotinoylamido-fenced tetraphenylporphyrin (PLLN/FeNFP), iron p...

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Veröffentlicht in:Journal of Oleo Science 2003, Vol.52(5), pp.269-276
Hauptverfasser: YAMAGUCHI, Aritomo, ISHINO, Tohru, MATSUKURA, Noriyoshi, KAWAKAMI, Hiroyoshi, ASAYAMA, Shoichiro, NAGAOKA, Shoji, YUASA, Makoto
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Sprache:eng
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Zusammenfassung:Novel superoxide dismutase (SOD) mimics, the macromolecule-ironporphyrin possessing poly(L-lysine) (PLLN) and iron tetraphenylporphyrin derivative are synthesized and their SOD activities are evaluated. The synthesis of PLLN-bound iron nicotinoylamido-fenced tetraphenylporphyrin (PLLN/FeNFP), iron pivaloylamido-fenced tetraphenylporphyrin (PLLN/FePFP) and iron tetraphenylporphyrin (PLLN/FeP) is conducted: The molar ratio of the iron tetraphenylporphyrin derivative to the structural unit of PLLN is found to be about 1/10 under the condition of this study. The rate constant, kcat, as indicator of SOD activity is about 106 M-1 s-1. PLLN/FePFP is shown far more capable of functioning as a SOD mimic compared to macromolecule-ironporphyrins, owing to creation of space for an active site due to the cationic polymer domain and fenced-groups.
ISSN:1345-8957
1347-3352
DOI:10.5650/jos.52.269