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Modulating Protein Function through Genetically Encoded Oxidative Chemistry.

Hengyu Li1, Alen Pavlič1, Noor E Ibrahim1

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, United States.

Journal of the American Chemical Society
|June 3, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

Researchers developed genetically encoded oxidative chemistry to control protein function in cells. This programmable system uses light-activated miniSOG to generate reactive oxygen species (ROS), enabling tunable modulation of protein activity and localization.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Biotechnology

Background:

  • Oxidative chemistry plays a role in cellular signaling but is not widely used for programmable protein regulation.
  • Existing methods for controlling protein function in cells have limitations in programmability and spatial organization.

Purpose of the Study:

  • To establish genetically encoded oxidative chemistry as a tunable framework for modulating protein function in living cells.
  • To demonstrate the spatial and temporal control of protein activity using light-activated reactive oxygen species (ROS).

Main Methods:

  • Utilized miniSOG, a genetically encoded photosensitizer, to generate ROS upon illumination.
  • Coupled miniSOG to specific intracellular contexts and proteins of interest, including redox reporters and ion channels.
  • Employed pathway-selective scavengers to investigate the selectivity of oxidative perturbation.

    • Main Results:

    • Demonstrated that controlled intracellular oxidation activates redox-sensitive TRP ion channels (TRPA1, TRPV1) and increases fluorescence of HyPerRed.
    • Showed that modulation strength and kinetics are tunable via illumination parameters, expression ratios, and subcellular localization.
    • Confirmed context-specific targeting of soluble and membrane proteins, with enhanced coupling to membrane effectors via membrane targeting.

    Conclusions:

    • Genetically encoded oxidative chemistry provides a versatile and spatially organized modality for engineering protein function.
    • This approach allows for precise, light-inducible control over protein activity within a defined cellular operating regime.
    • The framework is extendable to protein-proximal and native cellular settings, including modulation of endogenous proteins.