Membrane Protein Sorting: Proteoliposome Engineering with Cell‐Free Membrane Protein Synthesis: Control of Membrane Protein Sorting into Liposomes by Chaperoning Systems (Adv. Sci. 10/2018)

Ando, Mitsuru; Schikula, Shun; Sasaki, Yoshihiro; Akiyoshi, Kazunari

doi:10.1002/advs.201870062

Cited by 3 publications

(5 citation statements)

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“…[ 54 ] It has been reported that membrane proteins are incorporated into liposome membranes by PUREsystem expression in the presence of liposomes. [ 27,55 ] In this section, membrane protein expression was performed in the presence of lipid membrane‐coated particles, and the function of the membrane proteins incorporated into the surface of the particles was investigated. The Spike protein (S protein) of severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) was selected as the membrane protein in this study.…”

Section: Resultsmentioning

confidence: 99%

A Facile Method to Coat Nanoparticles with Lipid Bilayer Membrane: Hybrid Silica Nanoparticles Disguised as Biomembrane Vesicles by Particle Penetration of Concentrated Lipid Layers

Mizuta

Inoue

Sasaki

et al. 2023

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Natural membrane vesicles, including extracellular vesicles and enveloped viruses, participate in various events in vivo. To study and manipulate these events, biomembrane‐coated nanoparticles inspired by natural membrane vesicles are developed. Herein, an efficient method is presented to prepare organic–inorganic hybrid materials in high yields that can accommodate various lipid compositions and particle sizes. To demonstrate this method, silica nanoparticles are passed through concentrated lipid layers prepared using density gradient centrifugation, followed by purification, to obtain lipid membrane‐coated nanoparticles. Various lipids, including neutral, anionic, and cationic lipids, are used to prepare concentrated lipid layers. Single‐particle analysis by imaging flow cytometry determines that silica nanoparticles are uniformly coated with a single lipid bilayer. Moreover, cellular uptake of silica nanoparticles is enhanced when covered with a lipid membrane containing cationic lipids. Finally, cell‐free protein expression is applied to embed a membrane protein, namely the Spike protein of severe acute respiratory syndrome coronavirus 2, into the coating of the nanoparticles, with the correct orientation. Therefore, this method can be used to develop organic–inorganic hybrid nanomaterials with an inorganic core and a virus‐like coating, serving as carriers for targeted delivery of cargos such as proteins, DNA, and drugs.

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Section: Resultsmentioning

confidence: 99%

A Facile Method to Coat Nanoparticles with Lipid Bilayer Membrane: Hybrid Silica Nanoparticles Disguised as Biomembrane Vesicles by Particle Penetration of Concentrated Lipid Layers

Mizuta

Inoue

Sasaki

et al. 2023

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“…To overcome this issue, we recently developed a liposomal chaperoning system integrating a polyhistidine/nickel-chelate group pair (Figure 3b). 56 In the presence of nickel-chelating liposomes, N-terminal hexahistidine-fused membrane proteins were synthesized by the cell-free protein synthesis system. Owing to the high affinity between the nickel-chelate group and hexahistidine, the polypeptide of the membrane proteins interacted with the nickel-chelating liposome surface, which enhanced the incorporation of membrane proteins into the lipid membranes.…”

Section: Artificial Chaperone Systems For Proteinmentioning

confidence: 99%

“…Although this system was effective in the incorporation of membrane proteins, its integration efficiency was not sufficient. To overcome this issue, we recently developed a liposomal chaperoning system integrating a polyhistidine/nickel-chelate group pair (Figure b) . In the presence of nickel-chelating liposomes, N -terminal hexahistidine-fused membrane proteins were synthesized by the cell-free protein synthesis system.…”

Section: Artificial Chaperone Systems For Protein Foldingmentioning

confidence: 99%

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Artificial Molecular Chaperone Systems for Proteins, Nucleic Acids, and Synthetic Molecules

Nishimura

Akiyoshi

2020

Bioconjugate Chem.

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Molecular chaperones play critical roles in biological functions. They are closely involved in the maintenance of cell homeostasis, proper folding of proteins and nucleic acids, and inhibition of irreversible aggregation in denatured proteins. In addition to protein production, molecular chaperone function is widely recognized as important for peptide and protein drug delivery systems. Therefore, much effort has been made in recent decades to develop chaperone-mimetic molecules that have similar structures and biological functions to natural chaperones. These artificial molecular chaperone systems have been demonstrated to facilitate proper protein and nucleic acid folding, in addition to the formation of higher-order structures of synthetic molecules. Furthermore, the functions of these artificial systems show promising clinical applications in drug delivery and biomolecule detection. This topical review focuses on recent advances in the design, construction, characterization, and potential applications of different artificial molecular systems with distinct functional roles, such as the folding of water-soluble and membrane proteins, nucleic acids, and the self-assembly of synthetic molecules. Strategies used in the construction of some artificial molecule chaperone systems for proteins (such as pairs of amphiphilic molecules or self-assembled nanogels) and their applications as biomaterials are described. Specific examples from each design strategy are also highlighted to demonstrate the mechanisms, challenges, and limitations of the different artificial molecular systems. By highlighting the many new developments that have expanded the applications of the artificial chaperones beyond protein folding, this review aims to stimulate further studies on their design and applications.

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“…28 This approach has the benet of precise control over antigen presentation but comes with drawbacks including innate immunogenicity of the DNA origami structures. 29 As for liposome-based systems, previous studies have set precedent for the successful incorporation of integral membrane proteins into synthetic membranes, [30][31][32][33][34] including studies in which liposomes have modelled other viruses, such as HIV-1. [35][36][37] For SARS-CoV-2, recently natural and synthetic vesicles have been used to create VLPs by chemically conjugating the receptor-binding-domain (RBD) of the spike glycoprotein to membrane components.…”

Section: Introductionmentioning

confidence: 99%

SARS-CoV-2 virus-like-particles via liposomal reconstitution of spike glycoproteins

McColman,

Shkalla,

Sidhu

et al. 2023

Nanoscale Adv.

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Membrane Protein Sorting: Proteoliposome Engineering with Cell‐Free Membrane Protein Synthesis: Control of Membrane Protein Sorting into Liposomes by Chaperoning Systems (Adv. Sci. 10/2018)

Cited by 3 publications

References 0 publications

A Facile Method to Coat Nanoparticles with Lipid Bilayer Membrane: Hybrid Silica Nanoparticles Disguised as Biomembrane Vesicles by Particle Penetration of Concentrated Lipid Layers

A Facile Method to Coat Nanoparticles with Lipid Bilayer Membrane: Hybrid Silica Nanoparticles Disguised as Biomembrane Vesicles by Particle Penetration of Concentrated Lipid Layers

Artificial Molecular Chaperone Systems for Proteins, Nucleic Acids, and Synthetic Molecules

SARS-CoV-2 virus-like-particles via liposomal reconstitution of spike glycoproteins

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