ArticleNature materials2019
Rigid helical-like assemblies from a self-aggregating tripeptide.
Article in Nature materials, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 187 citations in OpenAlex.
- Free-standing ultrathin two-dimensional peptide crystals.Nature chemistry · 2026Article
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- Supramolecular engineering of amyloid-inspired tripeptide assemblies enabling tunable piezoelectricity.Nature communications · 2026Article
- Formation of S- and Z-twist supramolecular micro-ropes by peptide stereoisomers.Nature communications · 2026Article
- The ultrastiff crystals of mucic (galactaric) acid.Chemical science · 2026Article
- Antimicrobial Proteinoid Nanostructures via Thermal Condensation of L-Glutamic Acid and L-Tyrosine.Nanomaterials (Basel, Switzerland) · 2025Article
- Article
- Adaptive peptide dispersions enable drying-induced biomolecule encapsulation.Nature materials · 2025Article
- Chiroptical switching and strong circularly polarized luminescence in peptide supramolecular assemblies.Nature communications · 2025Article
- Microenvironment-responsive peptide hydrogels: molecular mechanisms, design and frontiers.Frontiers in bioengineering and biotechnology · 2025Review
- Amylum forms typical self-assembled amyloid fibrils.Science advances · 2024Article
- The Dimensionality of Hydrogen Bond Networks Induces Diverse Physical Properties of Peptide Crystals.ACS materials letters · 2024Article
- Semi-crystalline polymers with supramolecular synergistic interactions: from mechanical toughening to dynamic smart materials.Chemical science · 2024Review
- Assembly of short amphiphilic peptoids into nanohelices with controllable supramolecular chirality.Nature communications · 2024Article
- Piezoelectric nanomaterials: latest applications in biomedicine and challenges in clinical translation.Nanomedicine (London, England) · 2024Article
- Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity.Nature communications · 2023Article
- Peptide-derived coordination frameworks for biomimetic and selective separation.Analytical and bioanalytical chemistry · 2023Review
- Glycopeptide-Based Supramolecular Hydrogels Induce Differentiation of Adipose Stem Cells into Neural Lineages.ACS applied materials & interfaces · 2023Article
- Enzymatic polymerization of enantiomericNature communications · 2023Article
- Empirical Optimization of Peptide Sequence and Nanoparticle Colloidal Stability: The Impact of Surface Ligands and Implications for Colorimetric Sensing.ACS applied materials & interfaces · 2023Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The structural versatility, biocompatibility and dynamic range of the mechanical properties of protein materials have been explored in functional biomaterials for a wide array of biotechnology applications. Typically, such materials are made from self-assembled peptides with a predominant β-sheet structure, a common structural motif in silk and amyloid fibrils. However, collagen, the most abundant protein in mammals, is based on a helical arrangement. Here we show that Pro-Phe-Phe, the most aggregation-prone tripeptide of natural amino acids, assembles into a helical-like sheet that is stabilized by the dry hydrophobic interfaces of Phe residues. This architecture resembles that of the functional PSMα3 amyloid, highlighting the role of dry helical interfaces as a core structural motif in amyloids. Proline replacement by hydroxyproline, a major constituent of collagen, generates minimal helical-like assemblies with enhanced mechanical rigidity. These results establish a framework for designing functional biomaterials based on ultrashort helical protein elements.
Identifiers
What OpenQuestion holds
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.