This project is aimed at simulating the protein-protein interaction between p53 and MDM2. p53 is a protein that is crucial to cell aptosis and gene repair, making p53 a vital tumor suppressor. One of the functions of MDM2 in a cell is the down-regulation of p53. MDM2 binds and ubiquinates p53, targeting it for degradation via the proteasome.
Many new anti-cancer drugs are currently being developed which target the p53-MDM2 interface. These new drugs, called peptidomimetics, are much larger and more protein-like that previous small-molecule ligands, mimicking the chemical complementarity of p53 to block the binding site on MDM2. We are interested in using molecular simulation to study the mechanism by which peptidomimetics bind this interface, and to help design new classes of peptidomimetics to bind protein interfaces, such as spiroligomers.
List of Contributors
This project is managed by Prof. Vincent Voelz at Temple University.
Dr. Voelz's research focuses on using new simulation methods to unravel the mysteries of how proteins self-assemble into their functional folds, and to design folding and binding properties of proteins and peptide mimetics from first principles. The Voelz Lab participates in the Folding@home project, hosting two servers at Temple University. Dr. Voelz was formerly a postdoctoral scholar in the Vijay Pande lab at Stanford University.
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