Phosphorylation enzymes, which include the protein kinase CK2, play a critical role in controlling cell proliferation. Deregulated protein kinase activity is involved in numerous cancers, which has led to a recent surge in research on molecules that can inhibit enzyme activity. Today, known CK2 inhibitors are all organic compounds that neutralize enzymatic activity by binding to its active site, i.e., a particular region where the substrates bind together and enzymatic reactions take place.
The research by scientists at the Institute of Molecular Chemistry (CNRS/UPMC) and the Research Institute on Technologies and Life Science, whose results have just been published in the Chemistry and Biology journal, is very relevant. During the fruitful collaboration between chemists and biologists, they have identified a new class of CK2 inhibitors called polyoxometalates (POM), which are anionic inorganic metal oxide structures that have valuable catalytic properties and are primarily composed of metals (molybdenum and tungsten) and oxygen. To date, the molecules are the most powerful CK2 inhibitors, working at very low nanomolar concentrations. The researchers have also shown that the mode of POM action is completely new, albeit not yet fully understood. Unlike organic inhibitors, POM do not bind to the active site of the enzyme.
Research results have cleared the way for new areas of research, such as clearly identifying the action mechanism of the new molecules, finding the minimum molecular entity that can inhibit enzyme activity, and improving knowledge of the workings of the CK2 enzyme given its importance for health. In the long term, the results could pave the way for new approaches to the design of anticancer drugs.
