ArticleJournal of the Royal Society, Interface2013
Nanostructured functional films from engineered repeat proteins.
Article in Journal of the Royal Society, Interface, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 47 citations in OpenAlex.
- Engineered Protein-Based Ionic Conductors for Sustainable Energy Storage Applications.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Tuning the Dimensionality of Protein-Peptide Coassemblies to Build 2D Conductive Nanomaterials.ACS nano · 2025Article
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- Thickness Determination and Control in Protein-Based Biomaterial Thin Films.ACS applied bio materials · 2024Article
- Engineered Repeat Protein Hybrids: The New Horizon for Biologic Medicines and Diagnostic Tools.Accounts of chemical research · 2021Article
- Engineered protein-based functional nanopatterned materials for bio-optical devices.Nanoscale advances · 2019Article
- A Simple Approach to Design Proteins for the Sustainable Synthesis of Metal Nanoclusters.Angewandte Chemie (International ed. in English) · 2019Article
- Repeat proteins as versatile scaffolds for arrays of redox-active FeS clusters.Chemical communications (Cambridge, England) · 2019Article
- PyFolding: Open-Source Graphing, Simulation, and Analysis of the Biophysical Properties of Proteins.Biophysical journal · 2018Article
- Repeat protein scaffolds: ordering photo- and electroactive molecules in solution and solid state.Chemical science · 2016Article
- Article
- Control of repeat-protein curvature by computational protein design.Nature structural & molecular biology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fundamental advances in biotechnology, medicine, environment, electronics and energy require methods for precise control of spatial organization at the nanoscale. Assemblies that rely on highly specific biomolecular interactions are an attractive approach to form materials that display novel and useful properties. Here, we report on assembly of films from the designed, rod-shaped, superhelical, consensus tetratricopeptide repeat protein (CTPR). We have designed three peptide-binding sites into the 18 repeat CTPR to allow for further specific and non-covalent functionalization of films through binding of fluorescein labelled peptides. The fluorescence signal from the peptide ligand bound to the protein in the solid film is anisotropic, demonstrating that CTPR films can impose order on otherwise isotropic moieties. Circular dichroism measurements show that the individual protein molecules retain their secondary structure in the film, and X-ray scattering, birefringence and atomic force microscopy experiments confirm macroscopic alignment of CTPR molecules within the film. This work opens the door to the generation of innovative biomaterials with tailored structure and function.
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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.