Application of electrophoretic methods for detection of protein-porphyrin complexes.

Kowalska, Agnieszka; Kwiek, P.; Miłosz, Ewa; Gondek, Grzegorz; Romiszewska, Anna; Graczyk, Alfreda; Podhajska, Anna J.

doi:10.18388/abp.2003_3639

Cited by 12 publications

(3 citation statements)

References 16 publications

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“…Prior to separation the samples of proteins (12.5 lM or 25 lM) and PpIX (25 or 50 lM) were pre-incubated in buffer B (50 mM Hepes pH 6.8, 150 mM NaCl, 35% glycerol) 30 min/37°C in dark. After electrophoresis in standard 6% polyacrylamide gel under non-denaturing conditions the fluorescence of PpIX was detected by the detection System I [9,11,12].…”

Section: Detection Of Protein-ppix Complexes In Polyacrylamide Gelsmentioning

confidence: 99%

“…1A. The controls constituted of human serum albumin, a known blood carrier of multiple drugs [11][12][13][14] and GST. Of notice, only background fluorescence is registered for the negative controls, namely apotransferrin and GST, which excludes the probability of the GST modification to influence the PpIX binding to the investigated proteins.…”

Section: Protoporphyrin IX Co-migrates With the N-terminal Domain Of mentioning

confidence: 99%

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Targeting of p53 and its homolog p73 by protoporphyrin IX

et al. 2010

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Edited by Varda RotterKeywords: p53 p73 Protoporphyrin IX Photodynamic therapy Fluorescent band shift Fluorescence polarization a b s t r a c tThe p53 tumor suppressor is recognized as a promising target for anti-cancer therapies. We previously reported that protoporphyrin IX (PpIX) disrupts the p53/murine double minute 2 (MDM2) complex and leads to p53 accumulation and activation of apoptosis in HCT 116 cells. Here we show the direct binding of PpIX to the N-terminal domain of p53. Furthermore, we addressed the induction of apoptosis in HCT 116 p53-null cells by PpIX and revealed interactions between PpIX and p73. We propose that PpIX disrupts the p53/MDM2 or MDMX and p73/MDM2 complexes and thereby activates the p53-or p73-dependent cancer cell death.

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Section: Detection Of Protein-ppix Complexes In Polyacrylamide Gelsmentioning

confidence: 99%

Section: Protoporphyrin IX Co-migrates With the N-terminal Domain Of mentioning

confidence: 99%

Targeting of p53 and its homolog p73 by protoporphyrin IX

et al. 2010

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“…There have been several studies of protoporphyrin and chlorin e6 which are complexed with hydrophilic organic amine such as N -methyl- d -glucamine and arginine to improve their solubility in physiological solutions, while only few reports have been observed in the literature on pyropheophorbide- a derivatives complexed with hydrophilic organic amine used as a photosensitizer for PDT [ 13 – 14 ]. However, there is no research about salt formations between pyropheopheorbide- a and imidazole/piperazine.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Biological Evaluation of New Imidazolium and Piperazinium Salts of Pyropheophorbide-a for Photodynamic Cancer Therapy

Sengee

Badraa

Shim

2008

IJMS

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Abstract:We have designed imidazolium and piperazinium salts of pyropheophorbide-a in order to develop effective photosensitizers which have good solubility in polar and non polar media and to reveal the possible influences of the piperazine and imidazole moieties on the biological activities of pyropheophorbide-a. The phototoxicity of those pyropheophorbide-a salts against A549 cells was studied in vitro and compared with that of pyropheophorbide-a. The result showed that complexing piperazine and imidazole into pyropheophorbide-a decreases its dark toxicity without greatly decreasing phototoxicity and, enhances its phototoxicity without greatly increasing dark toxicity, respectively. This work not only describes novel amphiphilic salt complexes of pyropheophobide-a which retain the biological activities of the parent compound pyropheophorbide-a and could be effective candidate for PDT, but also reveals the possibility of developing effective photosensitizers by complexing imidazole and piperazine into other hydrophobic photosensitizers.

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In-Gel Staining of Proteins in Native Polyacrylamide Gel Electrophoresis Using Meso-Tetrakis(4-Sulfonatophenyl) Porphyrin

Divakar

Devi²,

Pennathur³

2012

Methods in Molecular Biology

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Protein identification in polyacrylamide gel electrophoresis (PAGE) requires post-electrophoretic steps like fixing, staining, and destaining of the gel, which are time-consuming and cumbersome. A new method for direct visualization of protein bands in PAGE has been developed using meso-tetrakis(4-sulfonatophenyl)porphyrin (TPPS) as a dye without the need for any post-electrophoretic steps; thus, separation and recovery of enzymes become much easier for further analysis. Activity staining was carried out to show that the biochemical activity of the enzymes was preserved after electrophoresis.

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Application of electrophoretic methods for detection of protein-porphyrin complexes.

Cited by 12 publications

References 16 publications

Targeting of p53 and its homolog p73 by protoporphyrin IX

Targeting of p53 and its homolog p73 by protoporphyrin IX

Synthesis and Biological Evaluation of New Imidazolium and Piperazinium Salts of Pyropheophorbide-a for Photodynamic Cancer Therapy

In-Gel Staining of Proteins in Native Polyacrylamide Gel Electrophoresis Using Meso-Tetrakis(4-Sulfonatophenyl) Porphyrin

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