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Protein-Labeling Reagents Selectively Activated by Copper(I).

Rong Cheng1, Yuki Nishikawa1, Takumi Wagatsuma2

  • 1Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.

ACS Chemical Biology
|May 15, 2024
PubMed
Summary

Researchers developed novel chemical biology probes to track copper ions (Cu+) in cells. These probes enable selective protein labeling, revealing insights into copper metabolism and cellular processes like cuproptosis.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Cell Biology

Background:

  • Copper is vital for biological processes, relying on redox cycling between Cu+ and Cu2+ states.
  • Understanding copper's biological roles requires tools for its selective detection in complex cellular environments.

Purpose of the Study:

  • To design and validate Cu+-responsive reagents for selective protein labeling.
  • To investigate copper ion dynamics and cellular responses using these novel probes.

Main Methods:

  • Development of conditional protein labeling reagents activated by Cu+ binding.
  • Utilizing oxidative bond cleavage to generate reactive quinone methides for covalent protein modification.
  • Employing gel- and imaging-based analyses for probe performance evaluation.
  • Applying conditional proteomics to identify protein targets in living cells.

Main Results:

  • A highly Cu+-selective probe was successfully designed and validated.
  • The probe detected dynamic changes in labile Cu+ concentrations within living cells.
  • Conditional proteomics revealed intramitochondrial Cu+ accumulation during cuproptosis.

Conclusions:

  • Cu+-responsive protein labeling is a powerful strategy for studying copper metabolism.
  • This approach provides novel insights into copper homeostasis and related cellular events.
  • The developed probes facilitate the elucidation of copper's biological functions.