ArticleChembiochem : a European journal of chemical biology2017
Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF.
Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Self-assembled proteomimetic (SAP) with antibody-like binding from short PNA-peptide conjugates.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Peptide foldamer-based inhibitors of the SARS-CoV-2 S protein-human ACE2 interaction.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Differential membrane binding of α/β-peptide foldamers: implications for cellular delivery and mitochondrial targeting.Australian journal of chemistry · 2023Article
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 2023Review
- Structure-Based Design of Peptides Targeting VEGF/VEGFRs.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Trimer-to-Monomer Disruption Mechanism for a Potent, Protease-Resistant Antagonist of Tumor Necrosis Factor-α Signaling.Journal of the American Chemical Society · 2022Article
- Modulating Angiogenesis by Proteomimetics of Vascular Endothelial Growth Factor.Journal of the American Chemical Society · 2022Article
- A Structural Overview of Vascular Endothelial Growth Factors Pharmacological Ligands: From Macromolecules to Designed Peptidomimetics.Molecules (Basel, Switzerland) · 2021Review
- Peptide Inhibitors of Vascular Endothelial Growth Factor A: Current Situation and Perspectives.Pharmaceutics · 2021Review
- Heterogeneous-Backbone Foldamer Mimics of Zinc Finger Tertiary Structure.Journal of the American Chemical Society · 2017Article
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Authors and funding
2 authors.
Funding
Abstract
Inhibition of specific protein-protein interactions is attractive for a range of therapeutic applications, but the large and irregularly shaped contact surfaces involved in many such interactions make it challenging to design synthetic antagonists. Here, we describe the development of backbone-modified peptides containing both α- and β-amino acid residues (α/β-peptides) that target the receptor-binding surface of vascular endothelial growth factor (VEGF). Our approach is based on the Z-domain, which adopts a three-helix bundle tertiary structure. We show how a two-helix "mini-Z-domain" can be modified to contain β and other nonproteinogenic residues while retaining the target-binding epitope by using iterative unnatural residue incorporation. The resulting α/β-peptides are less susceptible to proteolysis than is their parent α-peptide, and some of these α/β-peptides match the full-length Z-domain in terms of affinity for receptor-recognition surfaces on the VEGF homodimer.
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