Authors:

Brooklyn Cessna

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About Paper:

Normal cell function relies on specific Protein Protein Interaction (PPI) networks, which help maintain homeostasis within the cell. P53 is an important hub protein which interacts with various target proteins to create large PPIs. In some cases, the disruption of the PPI networks causes a "diseased state" within a cell, typically leading to apoptosis. P53 is an apoptosis inducer as well as a tumor suppressor, however if a mutation is present in the P53 pathway, then it may lead to the growth of cancer. P53 has been linked to 50% of all cancer developments. The purpose of this research is to computationally design protein pathway inhibitors of P53 to better understand its roles and interactions in the onset of cancer. Three of the target proteins being used in this study are CREB-Binding Protein (CBP), S100B, and SIRT-1. Each protein is widely studied and has known interactions with the C-terminal disordered region of P53. By computationally designing inhibitors that bind to the target proteins, we are able to examine P53 in its diseased-state. Through purification of the target proteins, we determined which designed inhibitors bind to each of the target proteins. SDS and Native Page gels were used to test purity of each protein. In addition, Fluorescence- Polarization (FP) was used to determine whether binding occurred between the inhibitor and target protein. Currently, the binding between the target protein and inhibitor has been tested and more are being designed. 111 UNIVERSITY OF OREGON • 2025 UNDERGRADUATE RESEARCH SYMPOSIUM TABLE OF CONTENTS

Source:

University of Oregon / 2025

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No topics listed

Co-authors:

Brooklyn Cessna