ArticleChembiochem : a European journal of chemical biology2022
Sulfono-γ-AApeptides as Protein Helical Domain Mimetics to Manipulate the Angiogenesis.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 3 citations in OpenAlex.
- Development of the Safe and Broad-Spectrum Aldehyde and Ketoamide Mpro inhibitors Derived from the Constrained α, γ-AA Peptide Scaffold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Structure-Based Design of Peptides Targeting VEGF/VEGFRs.Pharmaceuticals (Basel, Switzerland) · 2023Review
- An HR2-Mimicking Sulfonyl-γ-AApeptide Is a Potent Pan-coronavirus Fusion Inhibitor with Strong Blood-Brain Barrier Permeability, Long Half-Life, and Promising Oral Bioavailability.ACS central science · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Sulfono-γ-AApeptides recently developed in our group have been proven to be a new class of unnatural foldamer with well-defined helical structure and have been demonstrated to mimic protein helical domains and disrupt biomedically relevant protein-protein interactions (PPIs). Based on our design concept in a recent report, we discovered two similar sulfono-γ-AApeptides V2 and V3 which were designed to mimic the VEGF N-terminal helix α1 known to directly interact with VEGFRs. Interestingly, V2 was shown to possess the pro-angiogenic effect, whereas V3 was proved to be a potent inhibitor for angiogenesis. We speculate that the distinct angiogenesis signaling was due to the selective binding of the two molecules to VEGFR1 and VEGFR2, respectively. Together with their remarkable resistance to proteolytic degradation, relatively small sizes, and amenability to modification with diverse functional groups, V2 and V3 could serve as lead molecules for the development of potential therapeutic agents and molecular probes. These findings highlight sulfono-γ-AApeptides as an alternative paradigm to mimic the α-helical domain to modulate a wide variety of PPIs in the future.
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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.