ArticleNature communications2021
Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Cryo-EM for atomic characterization of supramolecular gels.Faraday discussions · 2025Article
- Small-angle scattering studies on diverse peptide-based nanotube and helical ribbon structures reveal distinct form and structure factors.Journal of applied crystallography · 2025Article
- Amphipathic Antimicrobial Peptides Illuminate a Reciprocal Relationship Between Self-assembly and Cytolytic Activity.Angewandte Chemie (International ed. in English) · 2025Article
- Fragment-Based Approach for Hierarchical Nanotube Assembly of Small Molecules in Aqueous Phase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Context-Dependent Heterotypic Assemblies of Intrinsically Disordered Peptides.Journal of the American Chemical Society · 2025Article
- Long-Range Proton Channels Constructed via Hierarchical Peptide Self-Assembly.Advanced materials (Deerfield Beach, Fla.) · 2024Article
- Interaction of Arginine-Rich Surfactant-like Peptide Nanotubes with Liposomes.Biomacromolecules · 2024Article
- Synthetic Collagen Hydrogels through Symmetric Self-Assembly of Small Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Backbone Hydration ofMolecular physics · 2024Article
- Autohydrolysis of Diglycine-Activated Succinic Esters Boosts Cellular Uptake.Angewandte Chemie (International ed. in English) · 2023Article
- Structural Elucidation of a Polypeptoid Chain in a Crystalline Lattice Reveals Key Morphology-Directing Role of the N-Terminus.ACS nano · 2023Article
- Advances in Peptide-Based Hydrogel for Tissue Engineering.Polymers · 2023Review
- Cell Adhesion Motif-Functionalized Lipopeptides: Nanostructure and Selective Myoblast Cytocompatibility.Biomacromolecules · 2023Article
- Intranuclear Nanoribbons for Selective Killing of Osteosarcoma Cells.Angewandte Chemie (International ed. in English) · 2022Article
- Co-assembled Coiled-Coil Peptide Nanotubes with Enhanced Stability and Metal-Dependent Cargo Loading.ACS omega · 2022Article
- Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Atomic structure of Lanreotide nanotubes revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides.International journal of molecular sciences · 2021Article
- Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide.Matter · 2021Article
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10 authors.
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Abstract
The exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the plasticity of quaternary structure in sequence-space and the lability of helical symmetry present significant challenges to the de novo design and structural analysis of such filaments. Here, we describe a rational approach to design self-assembling peptide nanotubes based on controlling lateral interactions between protofilaments having an unusual cross-α supramolecular architecture. Near-atomic resolution cryo-EM structural analysis of seven designed nanotubes provides insight into the designability of interfaces within these synthetic peptide assemblies and identifies a non-native structural interaction based on a pair of arginine residues. This arginine clasp motif can robustly mediate cohesive interactions between protofilaments within the cross-α nanotubes. The structure of the resultant assemblies can be controlled through the sequence and length of the peptide subunits, which generates synthetic peptide filaments of similar dimensions to flagella and pili.
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