Photosensitized Protein Damage by DiethyleneglycoxyP(V)tetrakis(p‐n‐butoxyphenyl)porphyrin Through Electron Transfer: Activity Control Through Self‐aggregation and Dissociation. (30th September 2021)

• Record Type: Journal Article
• Authors: Hirakawa, Kazutaka; Yoshida, Mami; Hirano, Toru; Nakazaki, Jotaro; Segawa, Hiroshi
• Is Part Of: Photochemistry and photobiology. Volume 98:Number 2(2022)
• Page Start: 434
• Page End: 441
• Publication Date: 2021-09-30
• Subjects: Photochemistry -- Periodicals; Light -- Physiological effect -- Periodicals; 541.35
• DOI: 10.1111/php.13517
• Languages: English
• ISSNs: 0031-8655

Abstract

Abstract: DiethyleneglycoxyP(V)tetrakis( p ‐ n‐ butoxyphenyl)porphyrin (EGP(V)TBPP) forms a self‐aggregation in an aqueous solution, and the photoexcited state of this molecule was effectively deactivated. Association with human serum albumin (HSA), a water‐soluble protein, causes dissociation of the self‐aggregation, resulting in recovery of the photosensitizer activity of EGP(V)TBPP. Under visible light irradiation, EGP(V)TBPP photosensitized HSA oxidation. The photosensitized singlet oxygen–generating activity of EGP(V)TBPP was confirmed by near‐infrared emission measurement. A singlet oxygen quencher, sodium azide, partially inhibited the HSA photodamage; however, the quenching effect was estimated to be 57%. Another 43% of the HSA photodamage could be explained by the electron transfer mechanism. The redox potential of EGP(V)TBPP and the calculated Gibbs energy of electron transfer from tryptophan to photoexcited EGP(V)TBPP demonstrated the possibility of HSA oxidation through electron extraction. Fluorescence lifetime measurements of EGP(V)TBPP verified the electron transfer from HSA. The photosensitizer activity of EGP(V)TBPP can be controlled through an association with biomolecules, such as protein, and the electron transfer–mediated biomolecule photooxidation plays an important role in photodynamic therapy under hypoxia. Abstract : The photosensitizer activity of diethyleneglycoxyP(V)tetrakis( p ‐ n ‐butoxyphenyl)porphyrin can be controlled through self‐aggregation and interaction with protein.