Preparation of Liposomes Surface-Loaded with Cationic Manganese Porphyrins as SOD Mimics

Makoto Yuasa, Kenichi Oyaizu, Akihiko Ogata, Noriyoshi Matsukura, Aritomo Yamaguchi

研究成果: Article

3 引用 (Scopus)

抄録

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.

元の言語English
ページ（範囲）233-239
ページ数7
ジャーナルJournal of Oleo Science
巻54
発行部数4
DOI
出版物ステータスPublished - 2005
外部発表Yes

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Liposomes
Porphyrins
Manganese
Phospholipids
Metalloporphyrins
Membranes
Ions
Fluorescence
Depolarization
Dimyristoylphosphatidylcholine
Water
Rate constants
Assays
Negative ions
Cytochromes c
Sodium
Superoxides
Proteins
Catalysts
tetrakis(N-methyl-4-pyridiniumyl)porphine manganese(III) complex

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

これを引用

Preparation of Liposomes Surface-Loaded with Cationic Manganese Porphyrins as SOD Mimics. / Yuasa, Makoto; Oyaizu, Kenichi; Ogata, Akihiko; Matsukura, Noriyoshi; Yamaguchi, Aritomo.

：: Journal of Oleo Science, 巻 54, 番号 4, 2005, p. 233-239.

研究成果: Article

Yuasa, M, Oyaizu, K, Ogata, A, Matsukura, N & Yamaguchi, A 2005, 'Preparation of Liposomes Surface-Loaded with Cationic Manganese Porphyrins as SOD Mimics', Journal of Oleo Science, 巻. 54, 番号 4, pp. 233-239. https://doi.org/10.5650/jos.54.233
Yuasa M, Oyaizu K, Ogata A, Matsukura N, Yamaguchi A. Preparation of Liposomes Surface-Loaded with Cationic Manganese Porphyrins as SOD Mimics. Journal of Oleo Science. 2005;54(4):233-239. https://doi.org/10.5650/jos.54.233
Yuasa, Makoto ; Oyaizu, Kenichi ; Ogata, Akihiko ; Matsukura, Noriyoshi ; Yamaguchi, Aritomo. / Preparation of Liposomes Surface-Loaded with Cationic Manganese Porphyrins as SOD Mimics. ：: Journal of Oleo Science. 2005 ; 巻 54, 番号 4. pp. 233-239.
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T1 - Preparation of Liposomes Surface-Loaded with Cationic Manganese Porphyrins as SOD Mimics

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AU - Yamaguchi, Aritomo

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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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