High-risk strain of human papillomavirus (HPV) have been identified as the main cause of cervical cancer by inducing infected epithelial cells. Specifically, the viral E6 protein associates with the human E6AP protein to form the E6-E6AP protein-protein complex, which causes the degradation of tumor suppressing p53 and subsequently, survival of the virus. Protein-protein interactions (PPIs) such as the E6-E6AP interaction, have been identified in many cellular processes as potential drug targets. New classes of drug-like compounds are needed for successful inhibition of such interactions. The Orchard lab has designed novel, amphiphilic, small molecule a-helix mimics that may be capable of inhibiting the E6-E6AP interaction by mimicking consecutive amino acid sequences from both faces of the E6AP alpha-helix which have been shown previously to be important for this binding event to occur. Successful inhibition of this PPI would allow infected cells to undergo apoptosis, avoiding any complex invasive clinical treatments. These compounds will be tested for their ability to inhibit the E6-E6AP interaction and characterized to determine their conformation during binding and in solution.

Alpha-helix mimetics as potential drugs for Human Papillomavirus (HPV)

253rd National Meeting (2017)

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