Au nanorods modulated NIR fluorescence and singlet oxygen generation of water soluble dendritic zinc phthalocyanine

The design of a dendrimeric-like diglycerol-tetrasubstituted Zn ( II ) phthalocyanine resulted in a remarkably water-soluble compound due to the presence of 16 hydroxyls. Several parameters relevant to evaluate the photodynamic efficiency of a potentiel photosensitizer such as: aggregation behavior, fluorescence properties, singlet oxygen generation, binding to a carrier protein model (Bovine Serum Albumin) and partition coefficient have been measured. Biocompatibility was demonstrated by dark cytotoxicity in in vitro experiments. The absence of phototoxicity can be explained by an elevated hydrophilicity. All the collected data have confirmed that this new substitution pattern is promising to be used on phthalocyanines aiming at being photodynamic therapy agents.

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Singlet Oxygen Generation from a Water-Soluble Hypervalent Iodine(V) Reagent AIBX and H2O2: An Access to Artemisinin

The Journal of Organic Chemistry ◽

10.1021/acs.joc.1c00596 ◽

2021 ◽

Author(s):

Hui-Jie Shen ◽

Ze-Nan Hu ◽

Chi Zhang

Keyword(s):

Singlet Oxygen ◽

Water Soluble ◽

Hypervalent Iodine ◽

Oxygen Generation ◽

Singlet Oxygen Generation

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Photosensitized damage of protein by fluorinated diethoxyphosphorus(V)porphyrin

Journal of Porphyrins and Phthalocyanines ◽

10.1142/s1088424612501258 ◽

2013 ◽

Vol 17 (01n02) ◽

pp. 56-62 ◽

Cited By ~ 6

Author(s):

Kazutaka Hirakawa ◽

Keito Azumi ◽

Yoshinobu Nishimura ◽

Tatsuo Arai ◽

Yoshio Nosaka ◽

...

Keyword(s):

Electron Transfer ◽

Human Serum Albumin ◽

Serum Albumin ◽

Singlet Oxygen ◽

Human Serum ◽

Transfer Mechanism ◽

Water Soluble ◽

Electron Transfer Mechanism ◽

Oxygen Generation ◽

Singlet Oxygen Generation

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.

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