Protein Chemical Modification Using Highly Reactive Species and Spatial Control of Catalytic Reactions

Research output: Contribution to journalReview articlepeer-review

3 Citations (Scopus)

Abstract

Protein bioconjugation has become an increasingly important research method for introducing artificial functions in to protein with various applications, including therapeutics and biomaterials. Due to its amphiphilic nature, only a few tyrosine residues are exposed on the protein surface. Therefore, tyrosine residue has attracted attention as suitable targets for site-specific modification, and it is the most studied amino acid residue for modification reactions other than lysine and cysteine residues. In this review, we present the progress of our tyrosine chemical modification studies over the past decade. We have developed several different catalytic approaches to selectively modify tyrosine residues using peroxidase, laccase, hemin, and ruthenium photocatalysts. In addition to modifying tyrosine residues by generating radical species through single-electron transfer, we have developed a histidine modification method that utilizes singlet oxygen generated by photosensitizers. These highly reactive chemical species selectively modify proteins in close proximity to the enzyme/catalyst. Taking advantage of the spatially controllable reaction fields, we have developed novel methods for site-specific antibody modification, detecting hotspots of oxidative stress, and target identification of bioactive molecules.

Original languageEnglish
Pages (from-to)95-105
Number of pages11
JournalChemical and Pharmaceutical Bulletin
Volume70
Issue number2
DOIs
Publication statusPublished - 2022 Feb 1

Keywords

  • Antibody chemical modification
  • Bioconjugation
  • Proximity labeling
  • Single-electron transfer
  • Tyrosine

Fingerprint

Dive into the research topics of 'Protein Chemical Modification Using Highly Reactive Species and Spatial Control of Catalytic Reactions'. Together they form a unique fingerprint.

Cite this