Related Experiment Video
Updated: Sep 28, 2025

11:20
An Integrated System to Remotely Trigger Intracellular Signal Transduction by Upconversion Nanoparticle-mediated Kinase Photoactivation
Published on: August 30, 2017
7.5K
μMap-Red: Proximity Labeling by Red Light Photocatalysis.
Benito F Buksh1,2, Steve D Knutson1,2, James V Oakley1,2
1Merck Center for Catalysis at Princeton University, Princeton, New Jersey08544, United States.
Journal of the American Chemical Society
|April 1, 2022
Summary
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.
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.

