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Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy
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Fast, Bright, and Reversible Fluorescent Labeling of Rhodamine-Binding Proteins.

Julian Kompa1, Lars J Dornfeld1, Nicola Porzberg1

  • 1Department of Chemical Biology, Max Planck Institute for Medical Research, Heidelberg 69120, Germany.

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|December 30, 2025
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This summary is machine-generated.

Researchers developed Rho-tag and SiR-tag, novel protein tags for bright, live-cell imaging. These tags enable rapid, membrane-permeable rhodamine labeling for advanced applications, including in vivo bioimaging.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Bioimaging

Background:

  • Rhodamine dyes are bright fluorescent probes for live-cell imaging.
  • Limited membrane permeability of rhodamine derivatives restricts their in vivo applications.

Purpose of the Study:

  • To engineer protein tags (Rho-tag and SiR-tag) for enhanced rhodamine dye labeling.
  • To overcome limitations in rhodamine dye permeability for improved bioimaging.

Main Methods:

  • Engineered protein tags derived from bacterial multidrug-resistant proteins.
  • Utilized unsubstituted (silicon) rhodamines for nanomolar affinity binding.
  • Demonstrated rapid, reversible, and fluorogenic labeling in mammalian cells.

Main Results:

  • Rho-tag and SiR-tag exhibit high affinity and specificity for rhodamines.
  • Unsubstituted rhodamines readily cross membranes, enabling rapid cell labeling.
  • Labeling is compatible with super-resolution microscopy and other tags (HaloTag7, SNAP-tag).
  • Successful in vivo imaging demonstrated in C. elegans embryos and zebrafish larvae.

Conclusions:

  • Rho-tag and SiR-tag facilitate efficient, permeable rhodamine-based bioimaging.
  • These tags offer a valuable tool for live-cell and in vivo fluorescence applications.
  • The combination of tag affinity and rhodamine properties enhances bioimaging capabilities.