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Protein Modification at Tyrosine with Iminoxyl Radicals
Katsuya Maruyama1, Takashi Ishiyama1, Yohei Seki1
1Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Journal of the American Chemical Society
|November 17, 2021
Summary
Researchers developed a new method for synthetic protein modifications (SPMs) targeting tyrosine residues. This technique allows for reversible control of protein function, offering new possibilities for biological research and therapeutics.
Area of Science:
- Chemical Biology
- Biochemistry
- Synthetic Chemistry
Background:
- Post-translational modifications (PTMs) are crucial for regulating protein function.
- Synthetic protein modifications (SPMs) can mimic PTMs, but reversible SPMs on hydrophobic residues are limited.
- Tyrosine (Tyr) residues present a challenge for developing reversible SPMs.
Purpose of the Study:
- To develop a tyrosine-selective synthetic protein modification (SPM) strategy.
- To achieve reversible control over protein function using SPMs.
- To explore applications in biological research and therapeutics.
Main Methods:
- Utilized persistent iminoxyl radicals generated from sterically hindered oximes.
- Investigated the reactivity and reversibility of iminoxyl radicals with tyrosine residues.
- Employed specific oximes (1f for stable, 1o for reversible modification) under mild conditions.
Main Results:
- Developed a tyrosine-selective SPM using iminoxyl radicals.
- Demonstrated reversible modification using oxime 1o, enabling on-demand control of protein function.
- Successfully altered enzymatic activity and antibody-antigen binding affinity via reversible Tyr modification.
Conclusions:
- Established a novel, reversible, tyrosine-selective covalent modification strategy.
- This SPM approach provides an on-demand ON/OFF switch for protein functions.
- Offers significant potential for advancing biological research and therapeutic development.
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