Reference of 2,6-PyridinedimethanolIn 2019 ,《Site-Specific Modification of Proteins through N-Terminal Azide Labeling and a Chelation-Assisted CuAAC Reaction》 appeared in Bioconjugate Chemistry. The author of the article were Inoue, Nozomu; Onoda, Akira; Hayashi, Takashi. The article conveys some information:
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%, RNase A: 90%). Kinetic anal. 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 mols. such as fluorophores, biotin, and polyethylene glycol. In the experiment, the researchers used many compounds, for example, 2,6-Pyridinedimethanol(cas: 1195-59-1Reference of 2,6-Pyridinedimethanol)
2,6-Pyridinedimethanol(cas: 1195-59-1) belongs to pyridine. The basicity and metallophilic high donor number of these π-deficient systems has long favored them as ligands in metal catalysis. The last decade saw pyridine assume a stronger role as functional group for directed C–H oxidation/activation.Reference of 2,6-Pyridinedimethanol
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