Near-infrared excited core-shell upconversion composites for living cells proteome labeling
Related Experiment Video
Updated: Oct 30, 2026

Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags
Published on: January 17, 2019
Chen Le1, Jiang Qianqian2, Jia Jingjing2
1School of Science, Dalian Maritime University, Dalian, Liaoning, 116026, China.
Abstract:
Near-infrared excitation effectively eliminates interference from intracellular visible-light-absorbing photosensitizers for living cells proteome labeling. Herein, a core-shell upconversion composites (CS-NaYF4@MOF) were developed for NIR activated proteome proximity labeling in living cells. A NIR-responsive photosensitizer was fabricated by in situ growth of a Cu-TCPP-based metal-organic framework (MOF) shell on Nd3+-sensitized core-shell upconversion nanoparticles. Upon 808 nm NIR excitation, the composites generate green upconversion luminescence to efficiently activate Cu(II) meso-Tetra(4-carboxyphenyl)porphine (Cu-TCPP) for reactive oxygen species production, enabling protein labeling in living cells with nucleophilic substrate. The characterizations confirm the successful formation of a crystalline MOF coating with homogeneous elemental distribution. Cellular assays reveal low photo-toxicity, allowing time- and concentration-dependent protein labeling under NIR light irradiation. By combining click chemistry and mass spectrometry, high-throughput proteome identification in living cells is successfully realized. This work not only extends the application of MOF-based materials in proteomics, but also offers a NIR excited strategy for living cells proteome labeling.
Related Concept Videos
Labeling DNA Probes
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)
Tagging and Fusion Proteins
Proteomics
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Imaging Biological Samples with Optical Microscopy
In optical microscopy, the specimen to be viewed is placed on a glass slide and clipped on the stage...

