5093-68-5

Upstream product

• 108-48-5 2,6-dimethylpyridine 
• 1073-23-0 2,6-lutidine N-oxide 
• 4808-64-4 4-nitro-2,6-lutidine-1-oxide 
• 5093-70-9 4-bromo-2,6-dimethylpyridine 

Relevant academic research and scientific papers

ANTAGONISTS OF THE ADENOSINE A2A RECEPTOR

The present invention relates to compounds of formula I shown below: wherein R0, R1, R2, R3 and A are each as defined in the application. The present invention also relates to processes for the preparation of these compounds, to pharmaceutical compositions comprising them, and to their use in the treatment of diseases or conditions in which adenosine A2a receptor activity is implicated, such as, for example, cancer.

Kinetic assay of the michael addition-like thiol-ene reaction and insight into protein bioconjugation

The chemical modification of proteins is a valuable technique in understanding the functions, interactions, and dynamics of proteins. Reactivity and selectivity are key issues in current chemical modification of proteins. The Michael addition-like thiol-ene reaction is a useful tool that can be used to tag proteins with high selectivity for the solvent-exposed thiol groups of proteins. To obtain insight into the bioconjugation of proteins with this method, a kinetic analysis was performed. New vinyl-substituted pyridine derivatives were designed and synthesized. The reactivity of these vinyl tags with L-cysteine was evaluated by UV absorption and high-resolution NMR spectroscopy. The results show that protonation of pyridine plays a key role in the overall reaction rates. The kinetic parameters were assessed in protein modification. The different reactivities of these vinyl tags with solvent-exposed cysteine is valuable information in the selective labeling of proteins with multiple functional groups. Tag! You're it! The Michael addition-like thiol-ene reaction between a pyridine-substituted vinyl group and the thiol of L-cysteine is evaluated by kinetic assay. Diverse reaction rates between different vinyl tags and free thiols are assessed, and the determined reactivity offers valuable information on protein bioconjugation.