ArticleAngewandte Chemie (International ed. in English)2018
Enzymatic Control of the Conformational Landscape of Self-Assembling Peptides.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
33 citing papers in PubMed.
- Enzyme-Activated Self-Assembling Peptides Mimicking Adiponectin Multimers for Nonalcoholic Fatty Liver Disease Therapy.ACS central science · 2026Article
- Controlling Nanonet Morphology via Residue-Specific Modulation of β-Hairpin Peptide for Enhanced Bacterial Trapping.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Article
- HydrogelFinder: A Foundation Model for Efficient Self-Assembling Peptide Discovery Guided by Non-Peptidal Small Molecules.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Unnatural Peptide Assemblies Rapidly Deplete Cholesterol and Potently Inhibit Cancer Cells.Journal of the American Chemical Society · 2024Article
- Injectable Thermo-Responsive Peptide Hydrogels and Its Enzyme Triggered Dynamic Self-Assembly.Polymers · 2024Article
- The Design of a Participatory Peptide Nucleic Acid Duplex Crosslinker to Enhance the Stiffness of Self-Assembled Peptide Gels.Angewandte Chemie (International ed. in English) · 2024Article
- Autohydrolysis of Diglycine-Activated Succinic Esters Boosts Cellular Uptake.Angewandte Chemie (International ed. in English) · 2023Article
- Advances in Self-Assembled Peptides as Drug Carriers.Pharmaceutics · 2023Review
- Enzyme-Responsive Peptide Thioesters for Targeting Golgi Apparatus.Journal of the American Chemical Society · 2022Article
- Enzymatic Noncovalent Synthesis for Targeting Subcellular Organelles.ChemPlusChem · 2022Review
- Supramolecular Nanomedicines ofFrontiers in chemistry · 2022Review
- Enzymatic noncovalent synthesis of peptide assemblies generates multimolecular crowding in cells for biomedical applications.Chemical communications (Cambridge, England) · 2021Review
- The Introduction of a Cysteine Residue Modulates The Mechanical Properties of Aromatic-Based Solid Aggregates and Self-Supporting Hydrogels.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Phosphobisaromatic motifs enable rapid enzymatic self-assembly and hydrogelation of short peptides.Soft matter · 2021Article
- Enzymatic Assemblies of Thiophosphopeptides Instantly Target Golgi Apparatus and Selectively Kill Cancer Cells*.Angewandte Chemie (International ed. in English) · 2021Article
- High-Throughput Peptide Derivatization toward Supramolecular Diversification in Microtiter Plates.ACS nano · 2021Article
- De novo design of a reversible phosphorylation-dependent switch for membrane targeting.Nature communications · 2021Article
- Fluorinated peptide biomaterials.Peptide science (Hoboken, N.J.) · 2021Article
- Enzymatically Forming Cell Compatible Supramolecular Assemblies of Tryptophan-Rich Short Peptides.Peptide science (Hoboken, N.J.) · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Post-translational modification is a common mechanism to affect conformational change in proteins, which in turn, regulates function. Herein, this principle is expanded to instruct the formation of supramolecular assemblies by controlling the conformational bias of self-assembling peptides. Biophysical and mechanical studies show that an engineered phosphorylation/dephosphorylation couple can affectively modulate the folding of amphiphilic peptides into a conformation necessary for the formation of well-defined fibrillar networks. Negative design principles based on the incompatibility of hosting residue side-chain point charge within hydrophobic environments proved key to inhibiting the peptide's ability to adopt its low energy fold in the assembled state. Dephosphorylation relieves this restriction, lowers the energy barrier between unfolded and folded peptide, and allows the formation of self-assembled fibrils that contain the folded conformer, thus ultimately enabling the formation of a cytocompatible hydrogel material.
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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.