ArticleACS chemical biology2015
Residue-Based Preorganization of BH3-Derived α/β-Peptides: Modulating Affinity, Selectivity and Proteolytic Susceptibility in α-Helix Mimics.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Slippery Liquid-Infused Porous Surfaces Infused with Thermotropic Liquid Crystals Enable Droplet-Based, Naked-Eye Reporting of Changes in Peptide Structure and Protease Activity.ACS applied materials & interfaces · 2025Article
- The Potential of Peptide-Based Inhibitors in Disrupting Protein-Protein Interactions for Targeted Cancer Therapy.International journal of molecular sciences · 2025Review
- Site-Specifically Modified Peptide Inhibitors of Protein Tyrosine Phosphatase 1B and T-Cell Protein Tyrosine Phosphatase with Enhanced Stability and Improved In Vivo Long-Acting Activity.ACS pharmacology & translational science · 2024Article
- Differential membrane binding of α/β-peptide foldamers: implications for cellular delivery and mitochondrial targeting.Australian journal of chemistry · 2023Article
- Structural Details of BH3 Motifs and BH3-Mediated Interactions: an Updated Perspective.Frontiers in molecular biosciences · 2022Review
- Discovery, development and application of drugs targeting BCL-2 pro-survival proteins in cancer.Biochemical Society transactions · 2021Review
- Discovery of Novel PTP1B Inhibitors Derived from the BH3 Domain of Proapoptotic Bcl-2 Proteins with Antidiabetic Potency.ACS medicinal chemistry letters · 2021Article
- Backbone Modifications of HLA-A2-Restricted Antigens Induce Diverse Binding and T Cell Activation Outcomes.Journal of the American Chemical Society · 2021Article
- Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity.Science advances · 2021Article
- Modulating Protein-Protein Interactions by Cyclic and Macrocyclic Peptides. Prominent Strategies and Examples.Molecules (Basel, Switzerland) · 2021Review
- Proteomimetic surface fragments distinguish targets by function.Chemical science · 2020Article
- Effects of Single α-to-β Residue Replacements on Recognition of an Extended Segment in a Viral Fusion Protein.ACS infectious diseases · 2020Article
- The Structural Biology of Bcl-xInternational journal of molecular sciences · 2019Review
- CPProtectides: Rapid uptake of well-folded β-hairpin peptides with enhanced resistance to intracellular degradation.Peptide science (Hoboken, N.J.) · 2019Article
- Differential Effects of βAngewandte Chemie (International ed. in English) · 2018Article
- Impact of Backbone Pattern and Residue Substitution on Helicity in α/β/γ-Peptides.Journal of the American Chemical Society · 2018Article
- Development of Potent, Protease-Resistant Agonists of the Parathyroid Hormone Receptor with Broad β Residue Distribution.Journal of medicinal chemistry · 2017Article
- Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF.Chembiochem : a European journal of chemical biology · 2017Article
- An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein-Protein Interactions.Angewandte Chemie (International ed. in English) · 2016Article
- Targeting recognition surfaces on natural proteins with peptidic foldamers.Current opinion in structural biology · 2016Review
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Authors and funding
6 authors.
Funding
Abstract
We report progress toward a general strategy for mimicking the recognition properties of specific α-helices within natural proteins through the use of oligomers that are less susceptible than conventional peptides to proteolysis. The oligomers contain both α- and β-amino acid residues, with the density of the β subunits low enough that an α-helix-like conformation can be adopted but high enough to interfere with protease activity. Previous studies with a different protein-recognition system that suggested ring-constrained β residues can be superior to flexible β residues in terms of maximizing α/β-peptide affinity for a targeted protein surface. Here, we use mimicry of the 18-residue Bim BH3 domain to expand the scope of this strategy. Two significant advances have been achieved. First, we have developed and validated a new ring-constrained β residue that bears an acidic side chain, which complements previously known analogues that are either hydrophobic or basic. Second, we have discovered that placing cyclic β residues at sites that make direct contact with partner proteins can lead to substantial discrimination between structurally homologous binding partners, the proteins Bcl-xL and Mcl-1. Overall, this study helps to establish that α/β-peptides containing ring-preorganized β residues can reliably provide proteolytically resistant ligands for proteins that naturally evolved to recognize α-helical partners.
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