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• W2134433520 endingPage "2034" @default.
• W2134433520 startingPage "2026" @default.
• W2134433520 abstract "ABSTRACT The growing resistance against antifungal agents has renewed the search for alternative treatment modalities, and antimicrobial photodynamic inactivation (PDI) is a potential candidate. The cationic porphyrin 5-phenyl-10,15,20-Tris( N -methyl-4-pyridyl)porphyrin chloride (TriP[4]) is a photosensitizer that in combination with light can inactivate bacteria, fungi, and viruses. For future improvement of the efficacy of PDI of clinically relevant fungi such as Candida albicans , we sought to understand the working mechanism by following the response of C. albicans exposed to PDI using fluorescence confocal microscopy and freeze-fracture electron microscopy. The following events were observed under dark conditions: TriP[4] binds to the cell envelope of C. albicans , and none or very little TriP[4] enters the cell. Upon illumination the cell membrane is damaged and eventually becomes permeable for TriP[4]. After lethal membrane damage, a massive influx of TriP[4] into the cell occurs. Only the vacuole membrane is resistant to PDI-induced damage once TriP[4] passes the plasma membrane. Increasing the incubation time of C. albicans with TriP[4] prior to illumination did not increase the influx of TriP[4] into the cell or the efficacy of PDI. After the replacement of 100% phosphate-buffered saline (PBS) by 10% PBS as the medium, C. albicans became permeable for TriP[4] during dark incubation and the efficacy of PDI increased dramatically. In conclusion, C. albicans can be successfully inactivated by the cationic porphyrin TriP[4], and the cytoplasmic membrane is the target organelle. TriP[4] influx occurred only after cell death." @default.
• W2134433520 created "2016-06-24" @default.
• W2134433520 creator A5020023657 @default.
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• W2134433520 date "2005-05-01" @default.
• W2134433520 modified "2023-10-12" @default.
• W2134433520 title "Mechanistic Study of the Photodynamic Inactivation of <i>Candida albicans</i> by a Cationic Porphyrin" @default.
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• W2134433520 doi "https://doi.org/10.1128/aac.49.5.2026-2034.2005" @default.
• W2134433520 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1087632" @default.
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