論文

査読有り 責任著者
2019年9月18日

Site-Specific Modification of Proteins through N-Terminal Azide Labeling and a Chelation-Assisted CuAAC Reaction

Bioconjugate Chemistry
  • Nozomu Inoue
  • ,
  • Akira Onoda
  • ,
  • Takashi Hayashi

30
9
開始ページ
2427
終了ページ
2434
記述言語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/acs.bioconjchem.9b00515

Site-specific modification of peptides and proteins is an important method for introducing an artificial function to the protein surface. Recently, we found that new bioconjugation reagents, 6-(azidomethyl)-2-pyridinecarbaldehyde (6AMPC) derivatives, allow specific N-terminal modification and enhance the reaction rate of the subsequent bioconjugation in a chelation-assisted CuAAC reaction. The N-terminal specific azide-labeling of bioactive peptides and proteins occurs under mild reaction conditions with 6AMPC derivatives (angiotensin I: 90%, ribonuclease A: 90%). Kinetic analysis of the CuAAC reaction with azide-labeled proteins reveals that the ligation is promoted in the presence of a copper-chelating pyridine moiety. Importantly, the introduction of an electron-donating methoxy group to the pyridine moiety further accelerates the CuAAC ligation. We demonstrate that this method enables site-specific conjugation of various functional molecules such as fluorophores, biotin, and polyethylene glycol.

リンク情報
DOI
https://doi.org/10.1021/acs.bioconjchem.9b00515
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/31436410
Scopus
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85072360038&origin=inward
Scopus Citedby
https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85072360038&origin=inward
ID情報
  • DOI : 10.1021/acs.bioconjchem.9b00515
  • ISSN : 1043-1802
  • eISSN : 1520-4812
  • PubMed ID : 31436410
  • SCOPUS ID : 85072360038

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