ArticleChemistry (Weinheim an der Bergstrasse, Germany)2016
γ-AApeptides as a New Class of Peptidomimetics.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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Who cites it
37 citing papers in PubMed.
- Peptide-based therapeutics targeting GPCRs: recent applications in the treatment of metabolic disorders.Frontiers in pharmacology · 2026Review
- Progress in the classification, optimization, activity, and application of antimicrobial peptides.Frontiers in microbiology · 2025Review
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- The discovery of cyclic γ-AApeptides as the promising ligands targeting EP2.Bioorganic & medicinal chemistry letters · 2023Article
- Article
- Emerging Pharmacotherapeutic Strategies to Overcome Undruggable Proteins in Cancer.International journal of biological sciences · 2023Review
- Sulfono-γ-AApeptides as Protein Helical Domain Mimetics to Manipulate the Angiogenesis.Chembiochem : a European journal of chemical biology · 2022Article
- Synthesis and Studies of Bulky Cycloalkyl α,β-Dehydroamino Acids that Enhance Proteolytic Stability.Organic letters · 2022Article
- Helical sulfono-γ-AApeptides with predictable functions in protein recognition.RSC chemical biology · 2022Review
- Peptidomimetic-based antibody surrogate for HER2.Acta pharmaceutica Sinica. B · 2021Article
- Towards a streamlined synthesis of peptides containing α,β-dehydroamino acids.Tetrahedron letters · 2021Article
- Dimeric lipo-α/sulfono-γ-AA hybrid peptides as broad-spectrum antibiotic agents.Biomaterials science · 2021Article
- Rational Design of Peptide-Based Inhibitors Disrupting Protein-Protein Interactions.Frontiers in chemistry · 2021Review
- Development of Bis-cyclic Imidazolidine-4-one Derivatives as Potent Antibacterial Agents.Journal of medicinal chemistry · 2020Article
- Rational Design and Synthesis of Right-Handed d-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein-Protein Interactions.The Journal of organic chemistry · 2020Article
- Aggregation-Induced Emissive and Circularly Polarized Homogeneous Sulfono-γ-AApeptide Foldamers.Advanced optical materials · 2020Article
- α-Helix-Mimicking Sulfono-γ-AApeptide Inhibitors for p53-MDM2/MDMX Protein-Protein Interactions.Journal of medicinal chemistry · 2020Article
- Impact of Dehydroamino Acids on the Structure and Stability of Incipient 3The Journal of organic chemistry · 2020Article
- Antibacterial activity of lipo-α/sulfono-γ-AA hybrid peptides.European journal of medicinal chemistry · 2020Article
- γ-AApeptides-based Small Molecule Ligands That Disaggregate Human Islet Amyloid Polypeptide.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Sequence-specific peptidomimetics are molecules that mimic the structure and function of peptides and proteins. With new backbones and molecular frameworks, peptidomimetics are of considerable interest in addressing challenges encountered in chemical biology and biomedical sciences. Based on the γ-PNA backbone, a new class of peptidomimetics - "γ-AApeptides" were recently developed. Both linear and cyclic γ-AApeptides can be synthesized with high efficiency. Compared with α-peptides, γ-AApeptides are resistant to enzymatic degradation, and amendable to diversification with a variety of chemical groups. Moreover, they could mimic primary and secondary structure, as well as the function of peptides, and show promise in biological applications, such as the development of new agents combating bacteria, cancer, and Alzheimer's disease. A few research outcomes of γ-AApeptides are highlighted in this Concept article, and a future perspective is also proposed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.