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oai:recercat.cat:20.500.14342/10212025-05-27T14:36:44Zcom_2072_482405com_2072_183628col_2072_482414

00925njm 22002777a 4500 dc Nonell, Santi author Rodríguez Amigo, Beatriz author Agut, Montserrat author Delcanale, Pietro author Juárez Jiménez, Jordi author Luque, F. Javier author Abbruzzetti, Stefania author Viappiani, Cristiano author 2017-01 Aggregation is a major problem for the anti-microbial photodynamic applications of hydrophobic photosensitizers since it strongly reduces the amount of singlet oxygen generated in aqueous solutions. Binding of hypericin (Hyp) to the milk whey protein β-lactoglobulin (βLG), occurring at the two hydrophobic cavities located at the interface of the protein homodimer, can be exploited to confer water-solubility and biocompatibility to the photosensitizer. The introduction of a small amount of the organic cosolvent dimethyl sulfoxide (DMSO) leads to a remarkable improvement of the photophysical properties of the complex Hyp–βLG by increasing its fluorescence emission and singlet oxygen photosensitization quantum yields. Surprisingly, the ability of the complex to photo-inactivate bacteria of the strain Staphylococcus aureus is strongly reduced in the presence of DMSO, despite the higher yield of photosensitization. The reasons for this apparently contradictory behavior are investigated, providing new insights into the use of carrier systems for hydrophobic photosensitizers. http://hdl.handle.net/20.500.14342/1021 https://doi.org/10.1039/C7TB00081B Fotosensibilització (Biologia) Sulfòxids Hydrophobic photosensitizers Dimeric protein Antibacterial treatment Tuning the local solvent composition at a drug carrier surface: the effect of dimethyl sulfoxide/water mixture on the photofunctional properties of hypericin–β-lactoglobulin complexes