ArticleChemical science2016
Repeat protein scaffolds: ordering photo- and electroactive molecules in solution and solid state.
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- 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
- Protein design under competing conditions for the availability of amino acids.Scientific reports · 2020Article
- Rationally Designed Protein Building Blocks for Programmable Hierarchical Architectures.Frontiers in chemistry · 2020Review
- Disease related single point mutations alter the global dynamics of a tetratricopeptide (TPR) α-solenoid domain.Journal of structural biology · 2020Article
- Engineered protein-based functional nanopatterned materials for bio-optical devices.Nanoscale advances · 2019Article
- Selective Immobilization of Fluorescent Proteins for the Fabrication of Photoactive Materials.Molecules (Basel, Switzerland) · 2019Article
- Repeat proteins as versatile scaffolds for arrays of redox-active FeS clusters.Chemical communications (Cambridge, England) · 2019Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The precise control over the organization of photoactive components at the nanoscale is one of the main challenges for the generation of new and sophisticated macroscopically ordered materials with enhanced properties. In this work we present a novel bioinspired approach using protein-based building blocks for the arrangement of photo- and electroactive porphyrin derivatives. We used a designed repeat protein scaffold with demonstrated unique features that allow for the control of their structure, functionality, and assembly. Our designed domains act as exact biomolecular templates to organize porphyrin molecules at the required distance. The hybrid conjugates retain the structure and assembly properties of the protein scaffold and display the spectroscopic features of orderly aggregated porphyrins along the protein structure. Finally, we achieved a solid ordered bio-organic hybrid thin film with anisotropic photoconductivity.
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Registered trials
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