Spectroscopic insights into BSA-mediated deaggregation of m-THPC.
Autor: | Kolman A; Faculty of Chemistry, Adam Mickiewicz University, Uniwersytetu Poznanskiego 8, Poznan, 61-614, Poland., Pedzinski T; Faculty of Chemistry, Adam Mickiewicz University, Uniwersytetu Poznanskiego 8, Poznan, 61-614, Poland., Lewandowska-Andralojc A; Faculty of Chemistry, Adam Mickiewicz University, Uniwersytetu Poznanskiego 8, Poznan, 61-614, Poland. alewand@amu.edu.pl.; Center for Advanced Technologies, Adam Mickiewicz University, Uniwersytetu Poznanskiego 10, Poznan, 61-614, Poland. alewand@amu.edu.pl. |
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Jazyk: | angličtina |
Zdroj: | Scientific reports [Sci Rep] 2024 Sep 27; Vol. 14 (1), pp. 22343. Date of Electronic Publication: 2024 Sep 27. |
DOI: | 10.1038/s41598-024-73266-2 |
Abstrakt: | Meta-tetra(hydroxyphenyl)chlorin (m-THPC) is among the most potent photosensitizers, known for its high singlet oxygen generation efficiency. However, its clinical effectiveness in photodynamic therapy (PDT) is compromised by its propensity to aggregate in aqueous solutions, adversely affecting its photophysical properties and therapeutic potential. A series of spectroscopic techniques, including UV-Vis absorption, fluorescence spectroscopy, and laser flash photolysis, revealed that m-THPC exhibits significant aggregation, particularly in MeOH-PBS mixtures with MeOH content below 30%. This aggregation adversely affects its photophysical properties leading to reduced fluorescence quantum yield and most importantly reducing its singlet oxygen quantum yield. This study introduces the use of bovine serum albumin (BSA) to counteract the aggregation of m-THPC, aiming to enhance its solubility, stability, and efficacy in physiological settings. Through advanced spectroscopic analyses we demonstrated that the m-THPC@BSA complex exhibits restored photophysical properties characteristic for monomeric form. Notably, the complex showed a significant restoration of the singlet oxygen quantum yield (Φ (© 2024. The Author(s).) |
Databáze: | MEDLINE |
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