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Published on: March 12, 2015
Harnessing Frémy's salt for tyrosine-directed bioconjugations
Zachary V Samuels1,2,3, Ava Stoddard1,3,4, Wei-Siang Mark Kao1,3
1Department of Chemistry, Hunter College, City University of New York New York NY 10065 USA bz102@hunter.cuny.edu.
RSC Advances
|January 22, 2026
Summary
This study introduces a novel bioconjugation method using Frémy's salt to modify tyrosine residues. This oxidation-controlled quinone ligation expands bioconjugation strategies beyond traditional lysine and cysteine modifications.
Area of Science:
- Chemical Biology
- Organic Chemistry
- Biochemistry
Background:
- Current bioconjugation primarily targets lysine and cysteine residues.
- Limited methods exist for modifying other amino acids like tyrosine.
Purpose of the Study:
- To develop a new bioconjugation strategy targeting tyrosine residues.
- To expand the scope of available bioconjugation tools.
Main Methods:
- Utilized Frémy's salt (potassium nitrosodisulfonate) for tyrosine oxidation.
- Developed a strain-promoted oxidation-controlled quinone ligation reaction.
- Employed trans-cyclooctene-bearing molecules as conjugation partners.
Main Results:
- Successfully achieved bioconjugation via tyrosine oxidation.
- Demonstrated the formation of 1,2-quinones from tyrosine residues.
- Established a novel ligation strategy between quinones and trans-cyclooctenes.
Conclusions:
- Frémy's salt enables efficient tyrosine modification for bioconjugation.
- The developed method offers an alternative to lysine/cysteine-based strategies.
- This approach broadens the possibilities for protein and peptide modification.
