ArticlePhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology2025
Unveiling role of serum albumin in disaggregation and cellular delivery of a near-infrared chlorophyll-based photosensitizer in breast cancer cells.
Article in Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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Who cites it
2 citing papers in PubMed.
- Photodynamic therapy in head and neck squamous cell carcinoma: immunomodulation and stromal targeting of cancer-associated fibroblasts.Translational oncology · 2026Review
- Folate-Functionalized Albumin-Containing Systems: Non-Covalent vs. Covalent Binding of Folic Acid.Pharmaceutics · 2025Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The efficacy of photosensitizer (PS) for photodynamic therapy of malignant tumors depends significantly on its interaction with serum proteins. Albumin binds non-covalently with hydrophilic and amphiphilic PSs. However, a clear understanding on role of albumin in delivery of PS in cancer cells is still lacking. We explored the role of albumin in disaggregation and cellular uptake of Cycloimide Purpurin-18 (CIPp-18), an amphiphilic near-infrared PS, in human breast carcinoma (MCF-7) cells. Results show that CIPp-18 added to fetal bovine serum (FBS) associates mainly with albumin and its aggregation in neat buffer is completely reversed by addition of bovine serum albumin (BSA). Under serum-enriched condition, CIPp-18 accumulated efficiently in cells and localized mainly in cell membrane and ER but not in lysosomes. Accumulation of CIPp-18 in cells was not affected by inhibitors of metabolic energy but partially inhibited at cold temperature. Confocal microscopy studies on uptake of CIPp-18 complexed to FITC-labeled BSA revealed significant colocalization of CIPp-18 and FITC-BSA in the distinct regions of cell membrane at 15 min after incubation, whereas at 90 min, FITC albumin localized independently in endocytic vesicles. Studies on binding of CIPp-18 with albumin using intrinsic tryptophan fluorescence of BSA and in silico docking reveal that CIPp-18 binds near Sudlow site I but away from tryptophan residue. Significant quenching of fluorescence of BSA-bound CIPp-18 by iodide ions further confirms that CIPp-18 binds at the surface of albumin. These results together demonstrate that the cellular uptake of albumin-bound CIPp-18 is mediated via facilitated diffusion involving dissociation of CIPp-18 from albumin prior to endocytosis. Further, the binding of CIPp-18 on the surface of albumin appears to play a crucial role in disaggregation and cellular uptake of CIPp-18.
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Registered trials
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