Structure-activity relationships of cancer-driven protein 

The human proteome is comprised of >20,000 proteins, though only a small proportion is currently targeted by FDA approved drugs. The absence of effective targeting approaches in combination with incomplete understanding of human biology are the two main factors that restrain expansion of the druggable proteome. In cancer, the majority of FDA approved oncology drugs are assigned to clear mechanistic protein targets, showing that insights into the structure-activity relationships of cancer-driven proteins is critical for drug development. Based on this knowledge, personalized cancer treatments are gradually replacing older standard-of-care therapeutic plans. My laboratory investigates the structural and functional features of immunomodulatory proteins with a key role in tumor survival, proliferation, and metastasis. Increasing our understanding of tumor escape mechanisms will reveal new protein targets and provide alternative approaches for precise targeting of advanced cancers. 

Of all the drug candidates that enter the drug development programs, only a small percent become approved. Ineffective protein targeting is one of the major unresolved issues and is related with undesired side-effects and low therapeutic efficacy. My laboratory applies novel approaches for targeting cancer-driver proteins. Our goal is to develop target-selective modulators that can be used either for therapeutic purposes or as agents to study the pathophysiological function(s) of the target protein. Our efforts are focused on targeting protein-protein interactions, allosteric regulation, proteins with enhanced flexibility and intrinsically disordered proteins. Since many challenging cancer-driven proteins belong to one of these groups, our plan reveals an immense potential for drug design and development.

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