ArticleProceedings of the National Academy of Sciences of the United States of America2019
Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 40 citations in OpenAlex.
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Exploring the temperature dependence of β-hairpin peptide self-assembly.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
- Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A Structural Analysis of Proteinaceous Nanotube Cavities and Their Applications in Nanotechnology.Nanomaterials (Basel, Switzerland) · 2022Review
- Imaging Orientation of a Single Molecular Hierarchical Self-Assembled Sheet: The Combined Power of a Vibrational Sum Frequency Generation Microscopy and Neural Network.The journal of physical chemistry. B · 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
- Supramolecular assembly of protein building blocks: from folding to function.Nano convergence · 2022Review
- Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide.Matter · 2021Article
- Cryo-EM is a powerful tool, but helical applications can have pitfalls.Soft matter · 2021Article
- Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials.Nature communications · 2021Article
- The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure.Nature communications · 2020Article
- Review
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Tandem repeat proteins exhibit native designability and represent potentially useful scaffolds for the construction of synthetic biomimetic assemblies. We have designed 2 synthetic peptides, HEAT_R1 and LRV_M3Δ1, based on the consensus sequences of single repeats of thermophilic HEAT (PBS_HEAT) and Leucine-Rich Variant (LRV) structural motifs, respectively. Self-assembly of the peptides afforded high-aspect ratio helical nanotubes. Cryo-electron microscopy with direct electron detection was employed to analyze the structures of the solvated filaments. The 3D reconstructions from the cryo-EM maps led to atomic models for the HEAT_R1 and LRV_M3Δ1 filaments at resolutions of 6.0 and 4.4 Å, respectively. Surprisingly, despite sequence similarity at the lateral packing interface, HEAT_R1 and LRV_M3Δ1 filaments adopt the opposite helical hand and differ significantly in helical geometry, while retaining a local conformation similar to previously characterized repeat proteins of the same class. The differences in the 2 filaments could be rationalized on the basis of differences in cohesive interactions at the lateral and axial interfaces. These structural data reinforce previous observations regarding the structural plasticity of helical protein assemblies and the need for high-resolution structural analysis. Despite these observations, the native designability of tandem repeat proteins offers the opportunity to engineer novel helical nanotubes. Moreover, the resultant nanotubes have independently addressable and chemically distinguishable interior and exterior surfaces that would facilitate applications in selective recognition, transport, and release.
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