Grison, CM, Miles, JA orcid.org/0000-0001-8839-9201, Robin, S et al. (2 more authors) (2016) An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein–Protein Interactions. Angewandte Chemie International Edition, 55 (37). pp. 11096-11100. ISSN 1433-7851
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
Keywords: | α-Helix-Mimetika; Foldamere; Inhibitoren; Peptidmimetika; Protein-Protein-Wechselwirkungen |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 30 Jun 2016 13:25 |
Last Modified: | 23 Jun 2023 22:09 |
Published Version: | https://doi.org/10.1002/anie.201604517 |
Status: | Published |
Publisher: | Wiley |
Identification Number: | 10.1002/anie.201604517 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:101737 |