《Bioinspired Nitroalkylation for Selective Protein Modification and Peptide Stapling》 was written by Mahesh, Sriram; Adebomi, Victor; Muneeswaran, Zilma P.; Raj, Monika. Safety of 2,6-Pyridinedimethanol And the article was included in Angewandte Chemie, International Edition in 2020. The article conveys some information:
Nitroalkanes react specifically with aldehydes, providing rapid, stable, and chemoselective protein bioconjugation. These nitroalkylated proteins mimic key post-translational modifications (PTMs) of proteins and can be used to understand the role of these PTMs in cellular processes. Demonstrated here is the substrate scope of this bioconjugation by attaching a variety of tags, such as NMR tags, fluorescent tags, affinity tags, and alkyne tags, to proteins. The structure and enzymic activity of modified proteins remain conserved after labeling. Notably, the nitroalkane group leads to easy characterization of proteins by mass spectrometry because of its distinct fingerprint pattern. Importantly, the nitro-alkylated peptides provide a new handle for site-selective fluorination of peptides, thus installing a specific probe to study peptide-protein interactions by 19F NMR spectroscopy. Furthermore, nitroalkane reagents can be used for the late-stage diversification of peptides and for the synthesis of peptide staples. After reading the article, we found that the author used 2,6-Pyridinedimethanol(cas: 1195-59-1Safety of 2,6-Pyridinedimethanol)
2,6-Pyridinedimethanol(cas: 1195-59-1) belongs to pyridine. When pyridine is adsorbed on oxide surfaces or in porous materials, the following species are commonly observed: (i) pyridine coordinated to Lewis acid sites, (ii) pyridine H-bonded to weakly acidic hydroxyls, and (iii) protonated pyridine. At high coverage, physisorbed pyridine and protonated dimers can also be observed.Safety of 2,6-Pyridinedimethanol
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