Topics
2021.06.01
Researchers have created a new nanometer-scale proximity labeling system that targets histidine res
Researcher
Shinichi Sato
Associate professorLife and Environments
- Mentor Information
- Professor
- Minoru Ishikawa (Graduate School of Life Sciences)
| Research Fields | Synthetic Organic Chemistry, Chemical Biology |
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| Research Subjects |
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| Academic Society Membership | The Chemical Society of Japan, The Pharmaceutical Society of Japan, The Japanese Peptide Society, International Chemical Biology Society |
| Research Outline | |
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Bioconjugation methods are techniques that have been extensively studied for covalent bond formation between a specific amino acid residue of a protein and a synthetic small compound. The methods are highly important in making protein-based biomaterials for therapeutic and biotechnology industries. In order to achieve reliable protein bioconjugation, the following requirements should be met: (1) stable covalent bond formation, (2) rapid reaction in aqueous solution, and (3) high conversion under physiological pH and mild temperature. We have developed tyrosine-specific bioconjugation methods with ruthenium photocatalysts, hemin, enzymes and electrochemistry. The relative hydrophobicity of tyrosine combined with the π−π stacking tendency of the aromatic rings results in generally low accessibility. We have developed site-selective protein modification by targeting surface-exposed tyrosine residues and applied to antibody site-selective functionalization. Furthermore, based on my unique methodology which controls the protein bioconjugation using single-electron transfer in proximity to the catalyst on the nanometer scale, we have developed a method for target-selective protein labeling in a protein mixture. This method enables us to identify target proteins of bioactive molecules. |
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