ArticleACS nano2019
Functional Coiled-Coil-like Assembly by Knob-into-Hole Packing of Single Heptad Repeat.
Article in ACS nano, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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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
4 citing papers in PubMed.
- Construction of Targeting-Peptide-Based Imaging Reagents and Their Application in Bioimaging.Chemical & biomedical imaging · 2024Review
- Structural Insights into the Dimeric Form ofBiomolecules · 2022Article
- Peptide-Protein Interactions: From Drug Design to Supramolecular Biomaterials.Molecules (Basel, Switzerland) · 2021Review
- Molecular design of stapled pentapeptides as building blocks of self-assembled coiled coil-like fibers.Science advances · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Coiled-coil peptides represent the principal building blocks for structure-based design of bionanomaterials. The sequence-structure relationship and precise nanoscale ordering of the coiled-coil helices originate from the knob-into-hole (KIH) packing of side chains. The helical interface stabilized by the KIH interaction is known to have chain lengths ranging from 30 to 1000 residues. Yet the shortest peptide required for oligomerization through KIH assembly is still unknown. Here, we report that through atomic resolution a minimal seven-residue amphipathic helix forms a different type of KIH motif, termed "supramolecular KIH packing", which confers an exceptional stability to the helical dimers. Significantly, at a low pH, the peptide self-assembles into nanofibers with coiled-coil architecture resembling the natural fibrous proteins. Furthermore, hierarchical ordering of the nanofibers affords lyotropic liquid crystals composed of a shortest natural helical sequence. Thus, this study expands the sequence space for a coiled-coil folding manifold and provides another paradigm for designer nanomaterials from minimal helical sequences.
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Registered trials
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