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Chemoproteomics analysis revealed photodynamic therapy (PDT) effect of Novel Photo-switchable Photosensitizer

ABSTRACT: The study titled "Dyad system of BOAHY-BODIPY Conjugates as Novel Photo-switchable Photosensitizer for Photodynamic Therapy" investigated the photodynamic therapy (PDT) potential of a compound that switches structures (Z form to E form) under UV irradiation. The compound generates reactive oxygen species (ROS) when exposed to light, with the Z form producing more ROS than the E form, leading to higher cytotoxicity. Chemoproteomics analysis revealed more protein modifications in the Z form, indicating greater ROS-induced changes compared to the E form. This suggests that the PDT effect and photo-switching ability can significantly impact biological processes, influencing genetic modifications and highlighting its potential in unbiased biomarker discovery for PDT studies.

INSTRUMENT(S): timsTOF Pro 2

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Jun-Seok Lee

PROVIDER: MSV000096072 | MassIVE | Sun Oct 13 21:54:00 BST 2024

REPOSITORIES: MassIVE

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Project description:Cysteine oxidation is a series of protein modifications caused by reactive oxygen species (ROS) in cells and can regulate protein functions and cellular activities. Comprehensive and site-specific characterization of the cysteine oxidation is critical for understanding the role of ROS regulating cellular events. Here we developed a chemoproteomics method to directly and systematically detect the reversible cysteine oxidation sites. Different from the commonly used methods for indirect detection of cysteine oxidation, this method allows for direct targeting of oxidized cysteine for MS analysis. The method was validated using small molecules containing oxidized cysteines and the whole cell lysate treated with the probe, demonstrating that it specifically targets reversible oxidized cysteines. In total, 3000-4000 proteins containing cysteine oxidation sites were identified from Jurkat, MCF7 and HEP G2 cells, respectively. Combining with multiplexed proteomics, we applied the method to quantify cysteine oxidation changes in the livers from mice fed with the high or low fat diet (HFD/LFD). It was found that the overall cysteine oxidation in mouse liver was dramatically upregulated with HFD, and the upregulation is correlated with protein distribution, functions, and the flanking residues of the oxidation sites. Many biological processes critical in the pathology of fatty liver diseases are also significantly enriched among the oxidized proteins with higher abundance in the HFD samples, suggesting the potential regulatory role of cysteine oxidation in the diseases. Additionally, the method was applied to study the cysteine oxidation change in THP-1 cells with the lipopolysaccharide treatment, and among >15000 cysteine oxidation sites quantified in THP-1 cells, many of them were upregulated under the treatment. For the oxidized proteins with upregulated oxidation sites, they are associated with inflammation and immune response, indicating the potential role of cysteine oxidation in regulating cellular response to bacterial infection. This chemoproteomics method can be widely applied to comprehensively study cysteine oxidation events in various samples.

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Chemoproteomics analysis revealed photodynamic therapy (PDT) effect of Novel Photo-switchable Photosensitizer

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