Recommended Citation
January 1, 2019.
Abstract
Myc is a popular transcription factor that is found in about 30% of human cancers. Along with being present in many cancers, it is also a potent oncogenic driver. Myc dimerizes with Max in order to promote transcription of genes that are associated with cellular proliferation, differentiation, and survival. In cancers that are Myc-driven, the Myc concentrations are higher than in healthy cells. Developing drugs in which impede Myc-Max dimerization has been difficult because there are many interactions that occur over large interfaces. This project hypothesizes that using molecular peptide ligands that adsorb to Myc at the Myc-Max dimer interface will disrupt the intermolecular interactions between Myc-Max. Molecular screening is used to identify cyclic peptide ligands that will have a high binding affinity to epitopes on Myc. By using the peptide ligands, they can be tested to measure their affinity to the Mac protein, the location of the binding on Myc, and its ability to inhibit the formation of the dimer by Myc-Max. By having this data, it then can be used to engineer peptides that are potent inhibitors of Myc-Max dimerization.
Mentor
Matt Idso
Lab site
Institute for Systems Biology (ISB)
Funding Acknowledgement
The 2018 STEM Teacher and Researcher Program and this project have been made possible through support from Chevron (www.chevron.com), the National Marine Sanctuary Foundation (www.marinesanctuary.org), the National Science Foundation through the Robert Noyce Program under Grant #1836335 and 1340110, the California State University Office of the Chancellor, and California Polytechnic State University in partnership with Institute for Systems Biology. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the author(s) and do not necessarily reflect the views of the funders.
URL: https://digitalcommons.calpoly.edu/star/494