The 7th Annual

NC State University

Undergraduate Summer Research Symposium

 

National Institutes of Health Undergraduate Scholarship Program (UGSP)


Abstracts are listed in alphabetical order by the last name of the corresponding author.

 

 

 

 

Student Author(s): 

Tran, Andy P.

Home Institution:

National Cancer Institute & NCSU

Program:

National Institutes of Health Undergraduate Scholarship Program (UGSP)

College:

PAMS

Department(s):

National Cancer Institute - Medical Oncology Branch

Research Mentor(s): 

Christine M. Hollander/National Cancer Institute

Larry Blanton/University Honors Program

Title of Presentation:

Evaluation of PH-domain Specificity of a New Akt Inhibitor



 

Lung cancer kills more than 170,000 people each year and it is the leading cause of cancer deaths in the United States. Of these lung cancer cases, 80% are identified as non-small cell lung cancer (NSCLC) and 20% are small cell lung cancer (SCLC). Recent studies show biochemical alterations such as activations of certain signal transduction pathways may be responsible for carcinogenesis and resistance to therapy. The activation of Akt-mTOR (serine/threonine kinase-mammalian target of rapamycin) pathway at S473 leads to the propagation of signals that are vital to cellular processes such as transcription, translation, cell cycle progression, and apoptosis. The role of this pathway in carcinogenesis and therapy resistance has inspired scientists to develop novel inhibitors that prevent the growth of tumors. Recent inhibitors of Akt at the ATP binding site have been shown to prevent tumor growth and also elicit potent cytotoxicity in vivo. However, these inhibitors often target multiple protein kinases because they share similarities in ATP binding sites. To address this, our group is developing a novel inhibitor that targets Akt at its pleckstrin homology (PH) domain. Using a virtual screening protocol, we have identified potential inhibitors of Akt from the ChemNavigator database. Our data shows that our lead compound, N-11 elicits favorable cytotoxicity in vitro against a number of cancer cell lines. Also, further experiments suggest that N-11’s inhibitory effects on Akt are through binding at its PH domain causing a displacement of Akt membrane localization and inactivation of this cancer pathway.

 

 

 

 

 

 

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