Oxidative damage induced by a novel porphyrin in tumour mitochondria and other model systems: Potential applications in photodynamic therapy

Chatterjee, Sarmishtha; Kamat, J.P.; Shetty, Shankar J.; Banerjee, Sukdeb; Srivastava, T.S.; Devasagayam, T.P.A.

doi:10.1016/s0969-806x(96)00121-1

Cited by 6 publications

(3 citation statements)

References 16 publications

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“…The photodynamic effect relates to the chemical action of the generated ROS on crucial cellular organelles and biomolecules, such as mitochondria [68], lipids, proteins, and nucleic acids [69][70][71]. 11) illustrates the generalized mechanism of alkylation of DNA with a simple quinone model.…”

Section: Photodynamic Agentsmentioning

confidence: 99%

Mechanisms of Anti-Cancer Agents Emphasis on Oxidative Stress and Electron Transfer

Kovacic

Osuna²

2000

CPD

149

105

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A large body of evidence has accumulated indicating involvement of oxidative stress (OS) in the mode of action of various bioactive substances, including those of the immune system. The data for anticancer drugs (main and miscellaneous) are summarized herein. Although diverse origins pertain, reactive oxygen species (ROS) are frequently generated by redox cycling via electron transfer (ET) groups, such as quinones (or phenolic precursors), metal complexes (or complexors), aromatic nitro compounds (or reduced products) and conjugated imines (or iminium species). We believe it is not coincidental that these functionalities are frequently found in anticancer agents or their metabolites. Generally, the ET moieties display reduction potentials in the physiologically active range. Often ROS are also implicated in more traditional rationales, namely, enzyme inhibition, membrane or DNA insult, and interference with DNA or protein synthesis. A multi-faceted approach to mechanism appears to be the most logical. Significantly, the unifying theme of ET-OS also applies to other drug categories, as well as to toxins, carcinogens, hormones, and enzymes. Since this theoretical framework aids in our understanding of drug action, it can serve as a useful tool in the design of more active and safer pharmaceuticals.

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Section: Photodynamic Agentsmentioning

confidence: 99%

Mechanisms of Anti-Cancer Agents Emphasis on Oxidative Stress and Electron Transfer

Kovacic

Osuna²

2000

CPD

149

105

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“…Tc-labelled meso-tetrakis [4- Tc-labelled T3, 4BCPP accumulates more in tumour tissue as compared with 99m Tclabelled T4CPP. These porphyrins have also been found to photodamage the membranes of mitochondria and microsomes via type I and type II mechanisms [11,[27][28][29][30]. The photodamage of membranes involves lipid peroxidation and enzyme inactivation [11,[28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Spectral investigations of the interaction of some porphyrins with bovine serum albumin

Chatterjee

Srivastava

2000

J. Porphyrins Phthalocyanines

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The binding of meso-tetrakis[4-(carboxymethyleneoxy)phenyl]porphyrin (T4CPP), meso-tetrakis[3-(carboxymethyleneoxy)phenyl]porphyrin (T3CPP) and meso-tetrakis[3,4-bis(carboxymethyl-eneoxy)phenyl]porphyrin (T3, 4BCPP) with bovine serum albumin (BSA) at pH 7.4 has been studied at 420 nm in detail. The results show hypochromicity along with a red shift in the Soret band of the porphyrins. This suggests that these porphyrins bind to BSA as monomers. Further analysis of these data supports the non-interactive binding of T4CPP and T3CPP with BSA and the cooperative binding of T3, 4BCPP with BSA. These binding data have been interpreted in terms of one specific binding site and several non-specific binding sites on BSA for the porphyrins. The absorption spectral changes of the porphyrins between 400 and 450 nm when titrated with BSA suggest that there is another specific binding site on BSA for the porphyrins. These two specific binding sites have also been supported by circular dichroism (CD) studies. The absorption spectral and CD studies on the interactions of the porphyrins with BSA further suggest that these interactions are dependent on the number and configuration of substituents in the phenyl groups of the porphyrins. The contact energy transfer from the aromatic amino acid residues tryptophan and tyrosine of BSA to the porphyrins in the BSA–porphyrin complexes has also been studied using fluorescence spectroscopy. These energy transfer data show the energy transfer from tryptophan to the porphyrins for their binding to site I of BSA and from tyrosine to the porphyrins for their binding to site II of BSA. Unfolding studies of the BSA–porphyrin systems indicate that the tertiary structure is essential for the binding of the porphyrins. A correlation between the accumulation of99 mTc -labelled T4CPP and T3, 4BCPP in tumour tissue and their binding at site II of BSA is possible. The interaction of the porphyrins can also be used as a model for mitochondrial interactions.

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“…The interactions of water-soluble cationic porphyrins and their metal-containing derivatives with DNA have been an interesting subject for years not only on account of their potential as excellent probes for the structure and dynamics of nucleic acids and proteins, [1][2][3][4] but also their applications in photodynamic therapy, [5][6][7][8][9] tumor imaging, [10,11] viral inactivation, [12,13] and artificial nucleases. [14,15] One of the most representative cationic porphyrins is meso-tetrakis(N-methylpyridinium-4-yl)porphyrin iodide, [(TMPyP)]I 4 , which can be coordinated with a variety of transition metals.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, Characterization, and DNA‐Binding and ‐Photocleavage Properties of Water‐Soluble Lanthanide Porphyrinate Complexes

Zhu

Wang

Leung

et al. 2011

Chemistry A European J

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A series of cationic lanthanide porphyrinate complexes of the general formula [(Por)Ln(H(2)O)(3)](+) (Ln(3+)=Yb(3+) and Er(3+)) were synthesized in moderate yields through the interaction of meso-pyridyl-substituted porphyrin free bases (H(2)Por) with [Ln{N(SiMe(3))(2)}(3)]·x[LiCl(thf)(3)], and the corresponding neutral derivatives [(Por)Ln(L(OMe))] (L(OMe)(-)=[(η(5)-C(5)H(5))Co{P(=O)(OMe)(2)}(3)](-)) were also prepared from [(Por)Ln(H(2)O)(3)](+) by the addition of the tripodal anion, L(OMe)(-), an effective encapsulating agent for lanthanide ions. Furthermore, the water-soluble lanthanide(III) porphyrinate complexes--including [(cis-DMPyDPP)Yb(H(2)O)(3)]Cl(3) (cis-DMPyDPP=5,10-bis(N-methylpyridinium-4'-y1)-15,20-di(phenyl)porphyrin), [(trans-DMPyDPP)Yb(H(2)O)(3)]Cl(3) (trans-DMPyDPP=5,15-bis(N-methylpyridinium-4'-y1)-10,20-di(phenyl)porphyrin), [(TMPyP)Yb(L(OMe))]I(4), and [(TMPyP)Er(L(OMe))]I(4) (TMPyP=tetrakis(N-methylpyridinium-4-y1)porphyrin)--were obtained by methylation of the corresponding complexes with methyl iodide and unambiguously characterized. The binding interactions and photocleavage activities of the water-soluble lanthanide(III) porphyrinate complexes towards DNA were investigated by UV-visible, fluorescence, and near-infrared luminescence spectroscopy, as well as circular dichroism and gel electrophoresis.

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Oxidative damage induced by a novel porphyrin in tumour mitochondria and other model systems: Potential applications in photodynamic therapy

Cited by 6 publications

References 16 publications

Mechanisms of Anti-Cancer Agents Emphasis on Oxidative Stress and Electron Transfer

Mechanisms of Anti-Cancer Agents Emphasis on Oxidative Stress and Electron Transfer

Spectral investigations of the interaction of some porphyrins with bovine serum albumin

Synthesis, Characterization, and DNA‐Binding and ‐Photocleavage Properties of Water‐Soluble Lanthanide Porphyrinate Complexes

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