Design of Hollow Protein Nanoparticles with Modifiable Interior and Exterior Surfaces

Kawakami, Norifumi; Kondo, Hiroki; Matsuzawa, Yuki; Hayasaka, Kaoru; Nasu, Erika; Sasahara, Kenji; Arai, Ryoichi; Miyamoto, Kenji

doi:10.1002/anie.201805565

Cited by 35 publications

(44 citation statements)

References 32 publications

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“…Besides, Arai et al created a WA20-foldon nanobuilding block by fusing the dimeric WA20 to the trimeric fibritin structure of bacteriophage T4, which could self-assemble to stable oligomeric structures with hexameric barrel and dodecameric tetrahedron (Kobayashi et al, 2015). Meanwhile, this method could be also used for design of more sophisticated 60-mer truncated icosahedral protein cages (TIP60) through fusing pentamer LSm and dimer MyoX-coil with a short linker (Kawakami et al, 2018).…”

Section: Non-specific Interaction Networkmentioning

confidence: 99%

Hierarchical Self-Assembly of Proteins Through Rationally Designed Supramolecular Interfaces

Sun

2020

Front. Bioeng. Biotechnol.

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With the increasing advances in the basic understanding of pathogenesis mechanism and fabrication of advanced biological materials, protein nanomaterials are being developed for their potential bioengineering research and biomedical applications. Among different fabrication strategies, supramolecular self-assembly provides a versatile approach to construct hierarchical nanostructures from polyhedral cages, filaments, tubules, monolayer sheets to even cubic crystals through rationally designed supramolecular interfaces. In this mini review, we will briefly recall recent progress in reconstituting protein interfaces for hierarchical self-assembly and classify by the types of designed protein-protein interactions into receptor-ligand recognition, electrostatic interaction, metal coordination, and non-specific interaction networks. Moreover, some attempts on functionalization of protein superstructures for bioengineering and/or biomedical applications are also shortly discussed. We believe this mini review will outline the stream of hierarchical self-assembly of proteins through rationally designed supramolecular interfaces, which would open minds in visualizing proteinprotein recognition and assembly in living cells and organisms, and even constructing multifarious functional bionanomaterials.

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Section: Non-specific Interaction Networkmentioning

confidence: 99%

Hierarchical Self-Assembly of Proteins Through Rationally Designed Supramolecular Interfaces

Sun

2020

Front. Bioeng. Biotechnol.

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“…[14][15][16] Common PNP fabrication methods include, among others, nab technologies, [17,18] coacervation, [19,20] and self-assembly. [21,22] Despite undoubtable progress in recent years, PNP technologies are still hampered by a range of drawbacks. While PNPs prepared via nab technologies have been implicated with decreased morbidity, [23] the processing conditions during particle preparation have been showed to cause protein denaturation.…”

Section: Doi: 101002/marc202000425mentioning

confidence: 99%

“…A small library of commercially available macromers was selected to investigate different sol/gel transitions. The first two macromers, 2 KDa O,O′-bis[2-(N-succinimidylsuccinylamino)ethyl]polyethylene glycol (PEG-NHS) and 4,7,10,13,16,19,22,25,32,35,38,41,44,47,50,53-hexadecaoxa-28,29-dithiahexapentacontanedioic acid di-N-succinimidyl ester (PEG-NHS-S), react the macromers' ester functional groups with the proteins' amine groups. This reaction completes after SPNPs are deposited by EHD jetting onto the collecting surface and then placed at 37 °C for 7 days.…”

Section: Protein Nanoparticles Are a Promising Approach For Nanotheramentioning

confidence: 99%

Multifunctional Synthetic Protein Nanoparticles via Reactive Electrojetting

Quevedo

Habibi

Gregory

et al. 2020

Macromol. Rapid Commun.

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Protein nanoparticles are a promising approach for nanotherapeutics, as proteins combine versatile chemical and biological function with controlled biodegradability. In this work, the development of an adaptable synthesis method is presented for synthetic protein nanoparticles (SPNPs) based on reactive electrojetting. In contrast to past work with electrohydrodynamic cojetting using inert polymers, the jetting solutions are comprised of proteins and chemically activated macromers, designed to react with each other during the processing step, to form insoluble nanogel particles. SPNPs made from a variety of different proteins, such as transferrin, insulin, or hemoglobin, are stable and uniform under physiological conditions and maintain monodisperse sizes of around 200 nm. SPNPs comprised of transferrin and a disulfide containing macromer are stimuli‐responsive, and serve as markers of oxidative stress within HeLa cells. Beyond isotropic SPNPs, bicompartmental nanoparticles containing human serum albumin and transferrin in two distinct hemispheres are prepared via reactive electrojetting. This novel platform provides access to a novel class of versatile protein particles with nanoscale architectures that i) can be made from a variety of proteins and macromers, ii) have tunable biological responses, and iii) can be multicompartmental, a prerequisite for controlled release of multiple drugs.

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“…For example, nanostructures of a barrel-shaped hexamer and a tetrahedron-like dodecamer self-assembled from protein nano-building blocks were reported by Kobayashi et al [69]. Quite curiously, the structures of a hyperstable 60-subunit protein icosahedron [71] and a truncated icosahedral protein composed of 60-mer fusion proteins (TIP60) [72] look like a virus particle and a soccer ball, respectively: once again the authors found the way home and produced nature mimetics. These strategies can be applied to create multimeric complexes of artificial lectins.…”

Section: Possible Procedures For Creating Artificial Lectinsmentioning

confidence: 99%

Lectin engineering: the possible and the actual

Hirabayashi

Arai

2019

Interface Focus.

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Lectins are a widespread group of sugar-binding proteins occurring in all types of organisms including animals, plants, bacteria, fungi and even viruses. According to a recent report, there are more than 50 lectin scaffolds (∼Pfam), for which three-dimensional structures are known and sugar-binding functions have been confirmed in the literature, which far exceeds our view in the twentieth century (Fujimoto et al. 2014 Methods Mol. Biol. 1200 , 579–606 ( doi:10.1007/978-1-4939-1292-6_46 )). This fact suggests that new lectins will be discovered either by a conventional screening approach or just by chance. It is also expected that new lectin domains including those found in enzymes as carbohydrate-binding modules will be generated in the future through evolution, although this has never been attempted on an experimental level. Based on the current state of the art, various methods of lectin engineering are available, by which lectin specificity and/or stability of a known lectin scaffold can be improved. However, the above observation implies that any protein scaffold, including those that have never been described as lectins, may be modified to acquire a sugar-binding function. In this review, possible approaches to confer sugar-binding properties on synthetic proteins and peptides are described.

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Design of Hollow Protein Nanoparticles with Modifiable Interior and Exterior Surfaces

Cited by 35 publications

References 32 publications

Hierarchical Self-Assembly of Proteins Through Rationally Designed Supramolecular Interfaces

Hierarchical Self-Assembly of Proteins Through Rationally Designed Supramolecular Interfaces

Multifunctional Synthetic Protein Nanoparticles via Reactive Electrojetting

Lectin engineering: the possible and the actual

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