A new route for the synthesis of 2-aminopyridines has been developed that merges C–H functionalization with amide alcoholysis. The key component of this method is the ability of a quinazolinone to template the chemo- and regioselective construction of a latent pyridine ring via site-selective olefinic C–H bond functionalization under Ru(II) catalysis. Thus, highly substituted 2-aminopyridines were prepared in good yield. Mechanistic studies provide insight into the mechanism of the key oxidative C–H activation/annulation process.
Tautomerizable heteroarenes, bearing multiple interconvertible nucleophilic centers exhibit high chemo- and regio- selective allylation irrespective of allylating agents used under Pd-catalysis. The achieved selectivity may be attributed to the dominant lactam form of heteroarenes and Pd-catalyzed intramolecular allylic substitution. A generalized green protocol for chemo- and regio-selective allylation of biologically relevant heteroarenes with allyl alcohols in dimethyl carbonate (DMC) as solvent was developed. Excellent selectivity was observed during intermolecular competition study demonstrating the differential nucleophilicity of tautomerizable heteroarenes and differential allyl palladium forming ability of a variety of allyl alcohols.
“Highly chemo- and regioselective allylic substitution with tautomerizable heteroarenes
Dinesh Kumar, Sandeep R. Vemula, Gregory R. Cook*
Green Chemistry 2015, accepted for publication
And that means the lab will be very busy with visiting students and intensive research. We would like to welcome our new group members who are coming in May. Joshua Nye is a Junior undergraduate student at NDSU and will be joining us to work on the HDAC inhibitor project. This summer we will host an REU student, Victoria Alao. She will be coming to Fargo from Western Illinois University to also work on our HDAC projects. And, finally, Anastasia de Celle, a high school student from Northern Cass High School, will be our PICNICS student for the summer. Welcome aboard!
We report, for the first time, that certain N-acetylthiourea derivatives serve as highly potent and isozyme selective activators for the recombinant form of human histone deacetylase-8 in the assay system containing Fluor-de-Lys as a fluorescent substrate. The experimental data reveals that such activating feature is manifested via decrease in the Km value of the enzyme’s substrate and increase in the catalytic turnover rate of the enzyme.
For more information, see: doi:10.1016/j.bmcl.2011.07.080