Cancer Chemical Systems Medicine
The Cancer Chemical Systems Medicine research group led by Krister Wennerberg focuses on gaining fundamental, novel understanding of cancers and their phenotypes by using a chemical systems biology approach. Through both 1) discovery and validation of novel oncology drug targets through the development of molecular probes and 2) utilization of collections of approved and investigational drugs on cancer cells, the research group aims to discover novel personalized therapeutic strategies and define and understand the molecular mechanisms driving the cancers, their drug responses and mechanisms of resistance.
Our group studies drug responses of cancer cells to functionally and therapeutically stratify cancers, to identify the underlying signals that drive the cancers and how effective personalized drug combinations can be predicted and established. A major research effort of our group is focused on the Individualized Systems Medicine in Cancer (ISM) program, a collaborative project among several FIMM research groups and Helsinki Central University Hospital (HUCH). For this program and other projects, we developed and applied the cancer cell Drug Sensitivity and Resistance Testing (DSRT) platform and analysis together with the High Throughput Biomedicine unit and the Aittokallio group at FIMM. This research effort has allowed us to functionally stratify cancers, identify new possible drug targets and to identify extended uses for existing drugs. The DSRT platform has also had a major impact on the research at FIMM in general and elsewhere with over 800 samples and cell lines screened to date and numerous articles published.
Furthermore, our group explores personalized cancer molecular profiling information to identify new therapeutic targets and small molecules inhibiting them. For this approach, we are exploring new ways of modulating mutant and non-mutant STAT3 signaling, personalized drug combinations targeting cancers with mutated RAS oncogenes, and developing inhibitors against the MKLP-1/MgcRacGAP/Ect2 protein complex.