ArticleACS macro letters2018
Self-Assembly of Electrostatic Cocrystals from Supercharged Fusion Peptides and Protein Cages.
Article in ACS macro letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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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
20 citing papers in PubMed.
- Programmed synthesis of mesoporous protein crystals in cellular reactors.Nature nanotechnology · 2026Article
- Self-assembly of 3D Ternary Crystals Consisting of Biological and Synthetic Nanoparticles.Biomacromolecules · 2026Article
- Review
- Colloidal Crystallization of Virus-Like Particles with Polycations.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Ferritin cages as building blocks for higher-order assembly through copper-sulfur bonds for HER analysis.RSC advances · 2024Article
- Emerging Landscape of Supercharged Proteins and Peptides for Drug Delivery.ACS pharmacology & translational science · 2024Review
- Article
- Advances in Peptide-Based Hydrogel for Tissue Engineering.Polymers · 2023Review
- Polypyrrole-Stabilized Polypeptide for Eco-Friendly Supercapacitors.International journal of molecular sciences · 2023Article
- Supercharged Protein Nanosheets for Cell Expansion on Bioemulsions.ACS applied materials & interfaces · 2023Article
- Understanding Supramolecular Assembly of Supercharged Proteins.ACS central science · 2022Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Substrate Partitioning into Protein Macromolecular Frameworks for Enhanced Catalytic Turnover.ACS nano · 2021Article
- Designed and biologically active protein lattices.Nature communications · 2021Article
- Protein cages as building blocks for superstructures.Engineering biology · 2021Article
- Agglomeration of Viruses by Cationic Lignin Particles for Facilitated Water Purification.ACS sustainable chemistry & engineering · 2020Article
- Hierarchical Self-Assembly of Proteins Through Rationally Designed Supramolecular Interfaces.Frontiers in bioengineering and biotechnology · 2020Review
- Virus capsid assembly across different length scales inspire the development of virus-based biomaterials.Current opinion in virology · 2019Review
- Functional protein nanostructures: a chemical toolbox.Chemical Society reviews · 2018Review
- Spontaneous Self-Organized Order Emerging From Intrinsically Disordered Protein Polymers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnologyReview
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Self-assembly is a convenient process to arrange complex biomolecules into large hierarchically ordered structures. Electrostatic attraction between the building blocks is a particularly interesting driving force for the assembly process, as it is easily tunable and reversible. Large biomolecules with high surface charge density, such as proteins and protein cages, are very promising building blocks due to their uniform size and shape. Assemblies of functional molecules with well-defined nanostructures have wide-ranging applications but are difficult to produce precisely by synthetic methods. Furthermore, obtaining highly ordered structures is an important prerequisite for X-ray structure analysis. Here we show how negatively charged ferritin and viral protein cages can adopt specific cocrystal structures with supercharged cationic polypeptides (SUPs, K72) and their recombinant fusions with green fluorescent protein (GFP-K72). The cage structures and recombinant proteins self-assemble in aqueous solution to large ordered structures, where the structure morphology and size are controlled by the ratio of oppositely charged building blocks and the electrolyte concentration. Both ferritin and viral cages form cocrystals with face centered cubic structure and lattice constants of 14.0 and 28.5 nm, respectively. The crystals are porous and the cationic recombinant proteins occupy the voids between the cages. Such systems resemble naturally occurring occlusion bodies and may serve as protecting agents as well as aid the structure determination of biomolecules by X-ray scattering.
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Registered trials
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