Document Type
Article
Publication Date
3-2009
Publication Source
Bioorganic and Medicinal Chemistry
Abstract
We previously described a series of 314-helical β-peptides that bind the hDM2 protein and inhibit its interaction with a p53-derived peptide in vitro. Here we present a detailed characterization of the interaction of these peptides with hDM2 and report two new β-peptides in which non-natural side chains have been substituted into the hDM2-recognition epitope. These peptides feature both improved affinity and inhibitory potency in fluorescence polarization and ELISA assays. Additionally, one of the new β-peptides also binds the hDM2-related protein, hDMX, which has been identified as another key therapeutic target for activation of the p53 pathway in tumors.
Inclusive pages
2038-2046
ISBN/ISSN
0968-0896
Document Version
Postprint
Copyright
Copyright © 2009 Elsevier Ltd. All rights reserved.
Publisher
Elsevier
Volume
17
Peer Reviewed
yes
Issue
5
Sponsoring Agency
National Institutes of Health (GM 74756) and the National Foundation for Cancer Research
eCommons Citation
Harker, Elizabeth A.; Daniels, Douglas S.; Guarracino, Danielle A.; and Schepartz, Alanna S., "Beta-peptides with improved affinity for hDM2 and hDMX" (2009). Chemistry Faculty Publications. 94.
https://ecommons.udayton.edu/chm_fac_pub/94
Comments
The document available for download is the authors' accepted manuscript, provided in compliance with the publisher's policy on self-archiving. Permission documentation is on file. To read the version of record, use the DOI provided.