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We developed μMap-Red, a novel red-light-activated proximity labeling platform. This tool enables precise protein labeling in complex biological samples and animal models, advancing biomolecular interaction studies.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioengineering

Background:

  • Proximity labeling techniques are crucial for studying biomolecular interactions.
  • Current methods face limitations in complex biological environments and animal models.

Purpose of the Study:

  • To introduce μMap-Red, a red-light-activated proximity labeling platform.
  • To enable protein labeling in challenging cellular and tissue microenvironments.

Main Methods:

  • Utilized a red-light-excited SnIV chlorin e6 catalyst to activate a phenyl azide biotin probe.
  • Validated photonic control of protein labeling in vitro through tissue layers.
  • Applied the platform in cellulo for EGFR microenvironment labeling.
  • Analyzed results using STED microscopy and quantitative proteomics.
  • Deployed μMap-Red in whole mouse blood for erythrocyte profiling.

Main Results:

  • Demonstrated photonically controlled protein labeling through multiple tissue layers.
  • Successfully labeled EGFR microenvironments in cellulo.
  • Profiled erythrocyte cell-surface proteins in whole mouse blood.
  • Validated platform performance with advanced microscopy and proteomics.

Conclusions:

  • μMap-Red represents a significant methodological advance for light-based proximity labeling.
  • The platform facilitates studies in complex tissue environments and animal models.
  • Enables deeper understanding of biomolecular interactions in vivo.