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An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein-Protein Interactions.
- Source :
- Angewandte Chemie International Edition; 9/5/2016, Vol. 55 Issue 37, p11096-11100, 5p
- Publication Year :
- 2016
-
Abstract
- A major current challenge in bioorganic chemistry is the identification of effective mimics of protein secondary structures that act as inhibitors of protein-protein interactions (PPIs). In this work, trans-2-aminocyclobutanecarboxylic acid ( tACBC) was used as the key β-amino acid component in the design of α/β/γ -peptides to structurally mimic a native α-helix. Suitably functionalized α/β/γ-peptides assume an α-helix-mimicking 12,13-helix conformation in solution, exhibit enhanced proteolytic stability in comparison to the wild-type α-peptide parent sequence from which they are derived, and act as selective inhibitors of the p53/ hDM2 interaction. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 14337851
- Volume :
- 55
- Issue :
- 37
- Database :
- Complementary Index
- Journal :
- Angewandte Chemie International Edition
- Publication Type :
- Academic Journal
- Accession number :
- 117807419
- Full Text :
- https://doi.org/10.1002/anie.201604517