ArticleACS central science2021
Origin of Proteolytic Stability of Peptide-Brush Polymers as Globular Proteomimetics.
Article in ACS central science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Amphipathic β‑Sheet-Forming Octapeptide Self-Assembly Using the Martini Potential Family.ACS omega · 2026Article
- Heterobifunctional proteomimetic polymers for targeted degradation of MYC and KRAS.Nature communications · 2026Article
- Protein-Like Polymers Targeting Keap1/Nrf2 as Therapeutics for Myocardial Infarction.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- The Role of Asparagine as a Gatekeeper Residue in the Selective Binding of Rare Earth Elements by Lanthanide-Binding Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Proteomimetic polymer blocks mitochondrial damage, rescues Huntington's neurons, and slows onset of neuropathology in vivo.Science advances · 2024Article
- Review
- Proteomimetic Polymers Trigger Potent Antigen-Specific T Cell Responses to Limit Tumor Growth.Journal of the American Chemical Society · 2024Article
- Inhibiting the Keap1/Nrf2 Protein-Protein Interaction with Protein-Like Polymers.Advanced materials (Deerfield Beach, Fla.) · 2024Article
- Controlled adsorption of multiple bioactive proteins enables targeted mast cell nanotherapy.Nature nanotechnology · 2024Article
- Thrombospondin-1 proteomimetic polymers exhibit anti-angiogenic activity in a neovascular age-related macular degeneration mouse model.Science advances · 2023Article
- Lipidation Alters the Structure and Hydration of Myristoylated Intrinsically Disordered Proteins.Biomacromolecules · 2023Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Peptide-brush polymers (PBPs), wherein every side-chain of the polymers is peptidic, represent a new class of proteomimetic with unusually high proteolytic resistance while maintaining bioactivity. Here, we sought to determine the origin of this behavior and to assess its generality via a combined theory and experimental approach. A series of PBPs with various polymer backbone structures were prepared and examined for their proteolytic stability and bioactivity. We discovered that an increase in the hydrophobicity of the polymer backbones is predictive of an elevation in proteolytic stability of the side-chain peptides. Computer simulations, together with small-angle X-ray scattering (SAXS) analysis, revealed globular morphologies for these polymers, in which pendant peptides condense around hydrophobic synthetic polymer backbones driven by the hydrophobic effect. As the hydrophobicity of the polymer backbones increases, the extent of solvent exposure of peptide cleavage sites decreases, reducing their accessibility to proteolytic enzymes. This study provides insight into the important factors driving PBP aqueous-phase structures to behave as globular, synthetic polymer-based proteomimetics.
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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.