2019年9月18日
Site-Specific Modification of Proteins through N-Terminal Azide Labeling and a Chelation-Assisted CuAAC Reaction
Bioconjugate Chemistry
- ,
- ,
- 巻
- 30
- 号
- 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
- ID情報
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- DOI : 10.1021/acs.bioconjchem.9b00515
- ISSN : 1043-1802
- eISSN : 1520-4812
- PubMed ID : 31436410
- SCOPUS ID : 85072360038