ArticleScience advances2016
Computationally designed peptides for self-assembly of nanostructured lattices.
Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed.
- Mesoporous peptide frameworks engineered from crystallizable collagen-mimetic peptide amphiphiles.Nature communications · 2026Article
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- 2D Assemblies Based on a Tetraphenylethylene D,L-Cyclic Peptide Scaffold.Angewandte Chemie (International ed. in English) · 2025Article
- Article
- Article
- Gold Nanoparticles Guided by Self-Assembling Peptides: From Sequence to Superstructure.Chembiochem : a European journal of chemical biology · 2025Review
- Peptide-based rigid nanorod-reinforced gelatin methacryloyl hydrogels for osteochondral regeneration and additive manufacturing.Nature communications · 2025Article
- Toward understanding biomolecular materials comprising intrinsically disordered proteinsMolecular systems design & engineering · 2025Review
- Architectural control of rod-coil block polypeptide thermoresponsive self-assemblyJournal of materials chemistry. B · 2025Article
- Ordered assemblies of peptide nanoparticles with only positive charge.Nature communications · 2024Article
- High Molecular Weight Protein-Like Semiflexible Chains via Bioorthogonal Polymerization of Coiled-Coil Peptides.Macromolecules · 2024Article
- Genetically Fusing Order-Promoting and Thermoresponsive Building Blocks to Design Hybrid Biomaterials.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Genetically Fused Resilin-like Polypeptide-Coiled Coil Bundlemer Conjugates Exhibit Tunable Multistimuli-Responsiveness and Undergo Nanofibrillar Assembly.Biomacromolecules · 2024Article
- Challenges and opportunities of poly(amino acid) nanomedicines in cancer therapy.Nanomedicine (London, England) · 2024Review
- Biomimetic Sequence-Templating Approach toward a Multiscale Modulation of Chromogenic Polymer Properties.Macromolecules · 2023Article
- Cyanine Dye Coupling Mediates Self-assembly of a pH Sensitive Peptide into Novel 3D Architectures.Angewandte Chemie (International ed. in English) · 2022Article
- Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering.Acta biomaterialia · 2022Review
- Computational Design of Single-Peptide Nanocages with Nanoparticle Templating.Molecules (Basel, Switzerland) · 2022Article
- Advanced Electron Microscopy of Nanophased Synthetic Polymers and Soft Complexes for Energy and Medicine Applications.Nanomaterials (Basel, Switzerland) · 2021Review
- De Novo Designed Peptide and Protein Hairpins Self-Assemble into Sheets and Nanoparticles.Small (Weinheim an der Bergstrasse, Germany) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Folded peptides present complex exterior surfaces specified by their amino acid sequences, and the control of these surfaces offers high-precision routes to self-assembling materials. The complexity of peptide structure and the subtlety of noncovalent interactions make the design of predetermined nanostructures difficult. Computational methods can facilitate this design and are used here to determine 29-residue peptides that form tetrahelical bundles that, in turn, serve as building blocks for lattice-forming materials. Four distinct assemblies were engineered. Peptide bundle exterior amino acids were designed in the context of three different interbundle lattices in addition to one design to produce bundles isolated in solution. Solution assembly produced three different types of lattice-forming materials that exhibited varying degrees of agreement with the chosen lattices used in the design of each sequence. Transmission electron microscopy revealed the nanostructure of the sheetlike nanomaterials. In contrast, the peptide sequence designed to form isolated, soluble, tetrameric bundles remained dispersed and did not form any higher-order assembled nanostructure. Small-angle neutron scattering confirmed the formation of soluble bundles with the designed size. In the lattice-forming nanostructures, the solution assembly process is robust with respect to variation of solution conditions (pH and temperature) and covalent modification of the computationally designed peptides. Solution conditions can be used to control micrometer-scale morphology of the assemblies. The findings illustrate that, with careful control of molecular structure and solution conditions, a single peptide motif can be versatile enough to yield a wide range of self-assembled lattice morphologies across many length scales (1 to 1000 nm).
Indexed as
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.