TY - JOUR
T1 - Preparation of Liposomes Surface-Loaded with Cationic Manganese Porphyrins as SOD Mimics
AU - Yuasa, Makoto
AU - Oyaizu, Kenichi
AU - Ogata, Akihiko
AU - Matsukura, Noriyoshi
AU - Yamaguchi, Aritomo
PY - 2005
Y1 - 2005
N2 - A water-soluble cationic 5,10,15,20-tetrakis(N-methylpyridinium-4-yl)porphinatomanganese(III) ion (MnT4MPyP) and water-insoluble 5,10,15,20-tetrakis(N-3-furyl)porphinatomanganese(III) ion (MnT3FuP) were prepared and ion-complexed with an anionic phospholipid membrane to enhance the circulation persistence of the porphyrin complexes in vivo. Fluorescence spectra and fluorescence depolarization experiments indicated MnT3FuP to be situated within the hydrophobic interior of the vesicle composed of the phospholipid membrane, while MnT4MPyP was anchored to the membrane by lipophilic tails with the metalloporphyrin head-group located on the interface between the membrance and aqueous solvent. SOD activity was determined by stopped-flow analysis and cytochrome c assay, which allowed the determination of IC50 and kcat values for the reaction of the metalloporphyrins with superoxide anion radical (O2-·). Sodium stearate-linked MnT4MPyP was the most effective catalyst as an SOD mimic to decompose O2-· at a second-order rate constant of 1.9 × 107 M-1s-1 in dimyristoylphosphatidylcholine (DMPC) liposomes. SOD activity of MnT3FuP was less than that of MnT4MPyP.
AB - A water-soluble cationic 5,10,15,20-tetrakis(N-methylpyridinium-4-yl)porphinatomanganese(III) ion (MnT4MPyP) and water-insoluble 5,10,15,20-tetrakis(N-3-furyl)porphinatomanganese(III) ion (MnT3FuP) were prepared and ion-complexed with an anionic phospholipid membrane to enhance the circulation persistence of the porphyrin complexes in vivo. Fluorescence spectra and fluorescence depolarization experiments indicated MnT3FuP to be situated within the hydrophobic interior of the vesicle composed of the phospholipid membrane, while MnT4MPyP was anchored to the membrane by lipophilic tails with the metalloporphyrin head-group located on the interface between the membrance and aqueous solvent. SOD activity was determined by stopped-flow analysis and cytochrome c assay, which allowed the determination of IC50 and kcat values for the reaction of the metalloporphyrins with superoxide anion radical (O2-·). Sodium stearate-linked MnT4MPyP was the most effective catalyst as an SOD mimic to decompose O2-· at a second-order rate constant of 1.9 × 107 M-1s-1 in dimyristoylphosphatidylcholine (DMPC) liposomes. SOD activity of MnT3FuP was less than that of MnT4MPyP.
KW - cationic metalloporphyrin
KW - liposome
KW - nano particle
KW - superoxide anion radical
KW - superoxide dismutase
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U2 - 10.5650/jos.54.233
DO - 10.5650/jos.54.233
M3 - Article
AN - SCOPUS:84876302213
VL - 54
SP - 233
EP - 239
JO - Journal of Oleo Science
JF - Journal of Oleo Science
SN - 1345-8957
IS - 4
ER -