Date of Submission

Spring 2017

Academic Programs and Concentrations

Chemistry

Project Advisor 1

Marc Koyack

Abstract/Artist's Statement

Estrogen Receptor Alpha (ER) is vital in the biology of breast carcinoma and is expressed in about 70% of breast cancers. Currently, patients with breast cancer are administered the antiestrogen, tamoxifen, a drug designed to induce the regression of tumor growth in ER(+) cancers. Unfortunately, many breast cancer patients quickly develop a resistance to tamoxifen upon continued administration. Previous research has demonstrated that the ER hinge region acts as an allosteric regulator of ER activity, and S100P has been shown to bind to this region. In breast tumor, S100P expression is seen specifically in cancerous cells. As such, S100P is often seen as an indicator of breast cancer malignancy. Fundamentally, targeting the ER-S100P interface is a good point of departure for developing novel anti-cancer agents. Using theoretical 3D models and homology binding studies , we were able to identify a beta peptide analogous to S100P that strongly bound the ER hinge region in silico. Such results suggest that beta S100P analogs might serve as innovative therapeutics capable of targeting and disrupting the ER-S100P interaction interface.

Open Access Agreement

On-Campus only

Creative Commons License

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

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