Rational Design and Synthesis of Right-Handed d-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein–Protein Interactions
Document Type
Article
Publication Date
2020
Digital Object Identifier (DOI)
https://doi.org/10.1021/acs.joc.0c00996
Abstract
Novel unprecedented helical foldamers have been effectively designed and synthesized. The homogeneous right-handed d-sulfono-γ-AApeptides represent a new generation of unnatural helical peptidomimetics, which have similar folding conformation to α-peptides, making them an ideal molecular scaffold to design α-helical mimetics. As demonstrated with p53-MDM2 PPI as a model application, the right-handed d-sulfono-γ-AApeptides reveal much-enhanced binding affinity compared to the p53 peptide. The design of d-sulfono-γ-AApeptides may provide a new and alternative strategy to modulate protein–protein interactions.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
The Journal of Organic Chemistry, v. 85, issue 16, p. 10552-10560
Scholar Commons Citation
Sang, Peng; Shi, Yan; Higbee, Pirada; Wang, Minghui; Abdulkadir, Sami; Lu, Junhao; Daughdrill, Gary W.; Chen, Jiandong; and Cai, Jianfeng, "Rational Design and Synthesis of Right-Handed d-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein–Protein Interactions" (2020). Molecular Biosciences Faculty Publications. 169.
https://digitalcommons.usf.edu/bcm_facpub/169
