197804-84-5Relevant academic research and scientific papers
Synthesis and protein kinase inhibitory activity of balanol analogues with modified benzophenone subunits
Lampe, John W.,Jagdmann Jr., G. Erik,Johnson, Mary George,Lai, Yen-Shi,Lowden, Christopher T.,Lynch, Michael P.,Mendoza, José S.,Murphy, Marcia M.,Wilson, Joseph W.,Ballas, Lawrence M.,Carter, Kiyomi,Biggers, Christopher K.,Darges, James W.,Davis, Jefferson E.,Hubbard, Frederick R.,Stamper, Mark L.,Defauw, Jean M.,Foglesong, Robert J.,Hall, Steven E.,Heerding, Julia M.,Hollinshead, Sean P.,Hu, Hong,Hughes, Philip F.
, p. 2624 - 2643 (2007/10/03)
A series of analogues of the protein kinase C (PKC) inhibitory natural product balanol which bear modified benzophenone subunits are described. The analogues were designed with the goal of uncovering structure -activity features that could be used in the development of PKC inhibitors with a reduced polar character compared to balanol itself. The results of these studies suggest that most of the benzophenone features found in the natural product are important for obtaining potent PKC inhibitory compounds. However, several modifications were found to lead to selective inhibitors of the related enzyme protein kinase A (PKA), and several specific modifications to the polar structural elements of the benzophenone were found to provide potent PKC inhibitors. In particular, it was found that replacement of the benzophenone carboxylate with bioisosteric equivalents could lead to potent analogues. Further, a tolerance for lipophilic substituents on the terminal benzophenone ring was uncovered. These results are discussed in light of recently available structural information for PKA.
The preparation of hindered biphenyls via the suzuki reaction
Johnson, Mary George,Foglesong, Robert J.
, p. 7001 - 7002 (2007/10/03)
The preparation of a number of hindered biphenyls is presented in which the arylboronate suffers from both steric crowding and electron withdrawing group deactivation.
