Efficient in Vitro Encapsulation of Protein Cargo by an Engineered Protein Container

Wörsdörfer, Bigna; Pianowski, Zbigniew; Hilvert, Donald

doi:10.1021/ja211011k

Cited by 110 publications

(136 citation statements)

References 27 publications

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“…In addition, Hilvert and coworkers reported that engineered nonviral protein capsids such as lumazine synthase from Aquifex aeolicus are also applicable as nano-carriers for proteins and DNA. [14][15][16] Currently, however, functional modification of natural protein capsules, such as plant viral capsids and virus-like lumazine synthase capsids, requires complicated technologies such as gene recombination and protein expression. Therefore, the reconstruction of virus-like nanocapsules from synthetic molecules would enhance their potential for molecular designs.…”

Section: Introductionmentioning

confidence: 99%

Guest-binding behavior of peptide nanocapsules self-assembled from viral peptide fragments

Matsuura

Watanabe

Matsushita

et al. 2013

Polym J

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The binding behavior of guests (dyes and DNA) into peptide nanocapsules formed via self-assembly of a 24-mer b-annulus peptide fragment obtained from the capsid protein of the tomato bushy stunt virus is reported. The pH dependence of the f potential of the peptide nanocapsules indicates that the C-and N-termini are directed to the exterior and interior of the nanocapsules, respectively. Equilibrium dialysis experiments with dyes and the peptide nanocapsules at pH 7 showed that the peptide nanocapsules tend to bind anionic dyes. Binding of sodium 8-anilinonaphthalene-1-sulfonate and uranine into the peptide nanocapsules minimally affected the size of the nanocapsules, whereas binding of other anionic dyes resulted in the formation of precipitates. In addition, binding of Thioflavin T to the b-annulus peptide promoted disassembly of the nanocapsules. Complexation of the b-annulus peptide with M13 phage DNA formed a core-shell nanosphere in which the DNA was encapsulated in the peptide assembly.

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Section: Introductionmentioning

confidence: 99%

Guest-binding behavior of peptide nanocapsules self-assembled from viral peptide fragments

Matsuura

Watanabe

Matsushita

et al. 2013

Polym J

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“…This selection formed the basis of a screen for mutants of AaLS that could better protect its host, presumably through improving encapsulation owing to increased negative charges on its interior surface. These improved capsids, called AaLS-13, can be isolated and loaded in vitro with monomers of GFP that have been mutated to bear 29 additional positively charged residues (Wörsdörfer et al 2011a), or even with similarly engineered human ferritin (Beck et al 2014). Ferritin is itself a small microcompartment, 12 nm in diameter, that binds and stores iron.…”

Section: Building Spatial Synthetic Biologymentioning

confidence: 99%

Building Spatial Synthetic Biology with Compartments, Scaffolds, and Communities

Polka

Hays

Silver

2016

Cold Spring Harb Perspect Biol

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Traditional views of synthetic biology often treat the cell as an unstructured container in which biological reactions proceed uniformly. In reality, the organization of biological molecules has profound effects on cellular function: not only metabolic, but also physical and mechanical. Here, we discuss a variety of perturbations available to biologists in controlling protein, nucleotide, and membrane localization. These range from simple tags, fusions, and scaffolds to heterologous expression of compartments and other structures that confer unique physical properties to cells. Next, we relate these principles to those guiding the spatial environments outside of cells such as the extracellular matrix. Finally, we discuss new directions in building intercellular organizations to create novel symbioses.

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“…For instance, Hilvert's group engineered an artificial protein container, a variant of lumazine synthase that forms icosahedral capsids capable of spontaneously encapsulating various proteins through electrostatic interactions [37,38].…”

Section: Drug Encapsulation Through Noncovalent Interactionsmentioning

confidence: 99%

Synthetic and Bioinspired Cage Nanoparticles for Drug Delivery

Deshayes

Gref

2014

Nanomedicine

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Nanotechnology has the potential to revolutionize drug delivery, but still faces some limitations. One of the main issues regarding conventional nanoparticles is their poor drug-loading and their early burst release. Thus, to overcome these problems, researchers have taken advantage of the host-guest interactions that drive some assemblies to form cage molecules able to strongly entrap their cargo and design new nanocarriers called cage nanoparticles. These systems can be classified into two categories: bioinspired nanosystems such as virus-like particles, ferritin, small heat shock protein: and synthetic host-guest supramolecular systems that require engineering to actually form supramolecular nanoassemblies. This review will highlight the recent advances in cage nanoparticles for drug delivery with a particular focus on their biomedical applications.

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Efficient in Vitro Encapsulation of Protein Cargo by an Engineered Protein Container

Cited by 110 publications

References 27 publications

Guest-binding behavior of peptide nanocapsules self-assembled from viral peptide fragments

Guest-binding behavior of peptide nanocapsules self-assembled from viral peptide fragments

Building Spatial Synthetic Biology with Compartments, Scaffolds, and Communities

Synthetic and Bioinspired Cage Nanoparticles for Drug Delivery

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