ArticleProceedings of the National Academy of Sciences of the United States of America2014
Exceptionally stable, redox-active supramolecular protein assemblies with emergent properties.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 111 citations in OpenAlex.
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- 2D Assemblies Based on a Tetraphenylethylene D,L-Cyclic Peptide Scaffold.Angewandte Chemie (International ed. in English) · 2025Article
- Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.Chemical science · 2024Article
- Understanding Supramolecular Assembly of Supercharged Proteins.ACS central science · 2022Article
- Pulse Dipolar Electron Paramagnetic Resonance Spectroscopy Reveals Buffer-Modulated Cooperativity of Metal-Templated Protein Dimerization.The journal of physical chemistry letters · 2022Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Substrate Partitioning into Protein Macromolecular Frameworks for Enhanced Catalytic Turnover.ACS nano · 2021Article
- Article
- Asymmetrizing an icosahedral virus capsid by hierarchical assembly of subunits with designed asymmetry.Nature communications · 2021Article
- Supramolecular Architectures of Nucleic Acid/Peptide Hybrids.International journal of molecular sciences · 2020Review
- Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction.Biochemistry · 2020Article
- Enzyme Assembly for Compartmentalized Metabolic Flux Control.Metabolites · 2020Review
- Rationally Designed Protein Building Blocks for Programmable Hierarchical Architectures.Frontiers in chemistry · 2020Review
- Hierarchical Self-Assembly of Proteins Through Rationally Designed Supramolecular Interfaces.Frontiers in bioengineering and biotechnology · 2020Review
- Engineering protein assemblies with allosteric control via monomer fold-switching.Nature communications · 2019Article
- Diverse protein assembly driven by metal and chelating amino acids with selectivity and tunability.Nature communications · 2019Article
- Article
- Supercharging enables organized assembly of synthetic biomolecules.Nature chemistry · 2019Article
- Controlling the Self-Assembly of Biomolecules into Functional Nanomaterials through Internal Interactions and External Stimulations: A Review.Nanomaterials (Basel, Switzerland) · 2019Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The designed assembly of proteins into well-defined supramolecular architectures not only tests our understanding of protein-protein interactions, but it also provides an opportunity to tailor materials with new physical and chemical properties. Previously, we described that RIDC3, a designed variant of the monomeric electron transfer protein cytochrome cb562, could self-assemble through Zn(2+) coordination into uniform 1D nanotubes or 2D arrays with crystalline order. Here we show that these 1D and 2D RIDC3 assemblies display very high chemical stabilities owing to their metal-mediated frameworks, maintaining their structural order in ≥90% (vol/vol) of several polar organic solvents including tetrahydrofuran (THF) and isopropanol (iPrOH). In contrast, the unassembled RIDC3 monomers denature in ∼30% THF and 50% iPrOH, indicating that metal-mediated self-assembly also leads to considerable stabilization of the individual building blocks. The 1D and 2D RIDC3 assemblies are highly thermostable as well, remaining intact at up to ∼70 °C and ∼90 °C, respectively. The 1D nanotubes cleanly convert into the 2D arrays on heating above 70 °C, a rare example of a thermal crystalline-to-crystalline conversion in a biomolecular assembly. Finally, we demonstrate that the Zn-directed RIDC3 assemblies can be used to spatiotemporally control the templated growth of small Pt(0) nanocrystals. This emergent function is enabled by and absolutely dependent on both the supramolecular assembly of RIDC3 molecules (to form a periodically organized structural template) and their innate redox activities (to direct Pt(2+) reduction).
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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.