Designing helical peptide inhibitors of protein–protein interactions
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Author(s) •
Rezaei Araghi, Raheleh
Keating, Amy E.
Date Issued
April 2016
Journal
Current Opinion in Structural Biology
Publisher
Elsevier
Citation
Rezaei Araghi, Raheleh, and Amy E Keating. “Designing Helical Peptide Inhibitors of Protein–protein Interactions.” Current Opinion in Structural Biology 39 (August 2016): 27–38 © 2016 Published by Elsevier Ltd
Version
Author's final manuscript
Abstract
Short helical peptides combine characteristics of small molecules and large proteins and provide an exciting area of opportunity in protein design. A growing number of studies report novel helical peptide inhibitors of protein-protein interactions. New techniques have been developed for peptide design and for chemically stabilizing peptides in a helical conformation, which frequently improves protease resistance and cell permeability. We summarize advances in peptide crosslinking chemistry and give examples of peptide design studies targeting coiled-coil transcription factors, Bcl-2 family proteins, MDM2/MDMX, and HIV gp41, among other targets.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/J.SBI.2016.04.001