Approximately 15% of all human tumors harbor mutant KRAS, a membrane-associated small GTPase and notorious oncogene. However, there are no drugs on the market that directly target KRAS and inhibit its aberrant functions. I will discuss our discovery of novel allosteric KRAS inhibitors that bind to activated KRAS with high affinity, disrupt effector binding, and inhibit signaling and cancer cell growth. I will highlight key chemical features of the compounds that are crtical for interactions with residues at the switch regions of KRAS, and talk about how molecular simulations and structure-based design can combine with cell and biophysical assays to facilate dicosvery.

High affinity KRAS inhibitors that disrupt effector binding

2019 Spring National Meeting

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