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Hidden route of protein damage through oxygen-confined photooxidation

Nature Communications · 2024 · Harm · Insufficient evidence

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The authors describe an "O2-confined photooxidation" mechanism in which oxygen captured in protein cavities is converted into multiple ROS, primarily mediated by tryptophan residues under blue light irradiation. They report that ROS generated in this way can …

Study snapshot

PublicationNature Communications · 2024
Study typeother
Reported directionHarm
Evidence ratingInsufficient

Abstract

Hidden route of protein damage through oxygen-confined photooxidation Kim S, Kim E, Park M, Kim SH, Kim BG, Na S, Sadongo VW, Wijesinghe WCB, Eom YG, Yoon G, Jeong H, Hwang E, Lee C, Myung K, Kim CU, Choi JM, Min SK, Kwon TH, Min D. Hidden route of protein damage through oxygen-confined photooxidation. Nat Commun. 2024 Dec 30;15(1):10873. doi: 10.1038/s41467- 024-55168-z. Abstract Oxidative modifications can disrupt protein folds and functions, and are strongly associated with human aging and diseases. Conventional oxidation pathways typically involve the free diffusion of reactive oxygen species (ROS), which primarily attack the protein surface. Yet, it remains unclear whether and how internal protein folds capable of trapping oxygen (O2) contribute to oxidative damage. Here, we report a hidden pathway of protein damage, which we refer to as O2-confined photooxidation. In this process, O2 is captured in protein cavities and subsequently converted into multiple ROS, primarily mediated by tryptophan residues under blue light irradiation. The generated ROS then attack the protein interior through constrained diffusion, causing protein damage. The effects of this photooxidative reaction appear to be extensive, impacting a wide range of cellular proteins, as supported by whole-cell proteomic analysis. This photooxidative mechanism may represent a latent oxidation pathway in human tissues directly exposed to visible light, such as skin and eyes. Open access paper: nature.com

Machine Enhanced Logic

AI evidence extraction

Structured fields below were generated from the paper’s abstract and metadata to make the evidence easier to inspect. Automated extraction may be incomplete or incorrect; verify important details against the original paper.

Study typeother
Effect directionharm
PopulationNot supplied
Sample sizeNot supplied
ExposureNot supplied
Evidence strengthInsufficientConfidence: 62% · Peer reviewed: yes

Main findings

The authors describe an "O2-confined photooxidation" mechanism in which oxygen captured in protein cavities is converted into multiple ROS, primarily mediated by tryptophan residues under blue light irradiation. They report that ROS generated in this way can attack protein interiors via constrained diffusion and that effects appear extensive across cellular proteins based on whole-cell proteomic analysis.

Outcomes measured

  • protein oxidative modifications/damage
  • reactive oxygen species (ROS) generation
  • whole-cell proteomic changes (cellular proteins impacted)

Limitations

  • No exposure parameters (e.g., wavelength, intensity, duration) are provided in the abstract.
  • Study design details (e.g., model system, sample size) are not stated in the abstract.
  • Relevance to human tissues is suggested but not directly demonstrated in the abstract.
View raw extracted JSON
{
  "study_type": "other",
  "exposure": {
    "band": null,
    "source": "blue light irradiation (visible light)",
    "frequency_mhz": null,
    "sar_wkg": null,
    "duration": null
  },
  "population": null,
  "sample_size": null,
  "outcomes": [
    "protein oxidative modifications/damage",
    "reactive oxygen species (ROS) generation",
    "whole-cell proteomic changes (cellular proteins impacted)"
  ],
  "main_findings": "The authors describe an \"O2-confined photooxidation\" mechanism in which oxygen captured in protein cavities is converted into multiple ROS, primarily mediated by tryptophan residues under blue light irradiation. They report that ROS generated in this way can attack protein interiors via constrained diffusion and that effects appear extensive across cellular proteins based on whole-cell proteomic analysis.",
  "effect_direction": "harm",
  "limitations": [
    "No exposure parameters (e.g., wavelength, intensity, duration) are provided in the abstract.",
    "Study design details (e.g., model system, sample size) are not stated in the abstract.",
    "Relevance to human tissues is suggested but not directly demonstrated in the abstract."
  ],
  "evidence_strength": "insufficient",
  "confidence": 0.62,
  "peer_reviewed_likely": "yes",
  "keywords": [
    "photooxidation",
    "blue light",
    "visible light",
    "protein cavities",
    "oxygen confinement",
    "reactive oxygen species",
    "tryptophan",
    "proteomics",
    "skin",
    "eyes"
  ],
  "suggested_hubs": []
}
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AI-extracted fields are generated from the abstract and metadata and may be incomplete or incorrect. This material is for informational purposes and is not medical advice.

Identifiers and source

DOI: 10.1038/s41467
PubMed: Not supplied

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