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Updated: Dec 22, 2025

Glycopeptide Capture for Cell Surface Proteomics
Published on: May 9, 2014
Enzyme-activated anchoring of peptide probes onto plasma membranes for selectively lighting up target cells
Julan Xia1, Sujuan Sun, Xianhua Wu
1State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan Provincial Key Laboratory of Biomacromolecular Chemical Biology, Hunan University, Changsha, 410082, P. R. China. cylei@hnu.edu.cn.
Abstract:
In a cellular microenvironment, numerous biomolecules are involved in various physiological and pathological processes. However, for the in-depth and comprehensive understanding of their roles at the molecular level, there is still a lack of detection techniques for the in situ tracking of these biomolecules in a local environment. Herein, we engineered a membrane insertion peptide (MIP) as an enzyme-activated membrane insertion peptide probe (eaMIP) that allowed the in situ tracking of the activity of target enzymes in living cells. In this strategy, the membrane insertion capacity of the MIP motif in each eaMIP was caged by appending a chemical moiety. In the presence of target enzymes, the caging moiety in each eaMIP was removed by enzymatic decaging, leading to the generation of active MIPs. The versatility of this design was demonstrated by lighting up different tumor cells with distinct fluorescence signal patterns, affording an alternative tool for clinical diagnostics, biochemical research and membrane engineering.
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