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Journal articles on the topic 'Protein nanocages'

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Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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1

Wang, Xiaoqiang, Haiyan Sun, Chengkun Liu, and Chao Wang. "A hemin-functionalized GroEL nanocage as an artificial peroxidase and its application in chromogenic detection." Analytical Methods 11, no. 16 (2019): 2197–203. http://dx.doi.org/10.1039/c9ay00201d.

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2

Silva, Filippo, Leopoldo Sitia, Raffaele Allevi, Arianna Bonizzi, Marta Sevieri, Carlo Morasso, Marta Truffi, Fabio Corsi, and Serena Mazzucchelli. "Combined Method to Remove Endotoxins from Protein Nanocages for Drug Delivery Applications: The Case of Human Ferritin." Pharmaceutics 13, no. 2 (February 6, 2021): 229. http://dx.doi.org/10.3390/pharmaceutics13020229.

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Protein nanocages represent an emerging candidate among nanoscaled delivery systems. Indeed, they display unique features that proved to be very interesting from the nanotechnological point of view such as uniform structure, stability in biological fluids, suitability for surface modification to insert targeting moieties and loading with different drugs and dyes. However, one of the main concerns regards the production as recombinant proteins in E. coli, which leads to a product with high endotoxin contamination, resulting in nanocage immunogenicity and pyrogenicity. Indeed, a main challenge in the development of protein-based nanoparticles is finding effective procedures to remove endotoxins without affecting protein stability, since every intravenous injectable formulation that should be assessed in preclinical and clinical phase studies should display endotoxins concentration below the admitted limit of 5 EU/kg. Different strategies could be employed to achieve such a result, either by using affinity chromatography or detergents. However, these strategies are not applicable to protein nanocages as such and require implementations. Here we propose a combined protocol to remove bacterial endotoxins from nanocages of human H-ferritin, which is one of the most studied and most promising protein-based drug delivery systems. This protocol couples the affinity purification with the Endotrap HD resin to a treatment with Triton X-114. Exploiting this protocol, we were able to obtain excellent levels of purity maintaining good protein recovery rates, without affecting nanocage interactions with target cells. Indeed, binding assay and confocal microscopy experiments confirm that purified H-ferritin retains its capability to specifically recognize cancer cells. This procedure allowed to obtain injectable formulations, which is preliminary to move to a clinical trial.
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3

Chesnokov, Yury, Andrey Mozhaev, Roman Kamyshinsky, Alexander Gordienko, and Liubov Dadinova. "Structural Insights into Iron Ions Accumulation in Dps Nanocage." International Journal of Molecular Sciences 23, no. 10 (May 10, 2022): 5313. http://dx.doi.org/10.3390/ijms23105313.

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Dps (DNA-binding protein from starved cells) is well known for the structural protection of bacterial DNA by the formation of highly ordered intracellular assemblies under stress conditions. Moreover, this ferritin-like protein can perform fast oxidation of ferrous ions and subsequently accumulate clusters of ferric ions in its nanocages, thus providing the bacterium with physical and chemical protection. Here, cryo-electron microscopy was used to study the accumulation of iron ions in the nanocage of a Dps protein from Escherichia coli. We demonstrate that Fe2+ concentration in the solution and incubation time have an insignificant effect on the volume and the morphology of iron minerals formed in Dps nanocages. However, an increase in the Fe2+ level leads to an increase in the proportion of larger clusters and the clusters themselves are composed of discrete ~1–1.5 nm subunits.
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4

Li, Feng, Yanhua Chen, Huiling Chen, Wei He, Zhi-Ping Zhang, Xian-En Zhang, and Qiangbin Wang. "Monofunctionalization of Protein Nanocages." Journal of the American Chemical Society 133, no. 50 (December 21, 2011): 20040–43. http://dx.doi.org/10.1021/ja207276g.

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5

Theil, Elizabeth C. "Ferritin protein nanocages—the story." Nanotechnology Perceptions 8, no. 1 (March 30, 2012): 7–16. http://dx.doi.org/10.4024/n03th12a.ntp.08.01.

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6

Kim, Seong A., Seohyun Kim, Gi Beom Kim, Jiyoung Goo, Nayeon Kim, Yeram Lee, Gi-Hoon Nam, et al. "A Multivalent Vaccine Based on Ferritin Nanocage Elicits Potent Protective Immune Responses against SARS-CoV-2 Mutations." International Journal of Molecular Sciences 23, no. 11 (May 30, 2022): 6123. http://dx.doi.org/10.3390/ijms23116123.

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The SARS-CoV-2 pandemic has created a global public crisis and heavily affected personal lives, healthcare systems, and global economies. Virus variants are continuously emerging, and, thus, the pandemic has been ongoing for over two years. Vaccines were rapidly developed based on the original SARS-CoV-2 (Wuhan-Hu-1) to build immunity against the coronavirus disease. However, they had a very low effect on the virus’ variants due to their low cross-reactivity. In this study, a multivalent SARS-CoV-2 vaccine was developed using ferritin nanocages, which display the spike protein from the Wuhan-Hu-1, B.1.351, or B.1.429 SARS-CoV-2 on their surfaces. We show that the mixture of three SARS-CoV-2 spike-protein-displaying nanocages elicits CD4+ and CD8+ T cells and B-cell immunity successfully in vivo. Furthermore, they generate a more consistent antibody response against the B.1.351 and B.1.429 variants than a monovalent vaccine. This leads us to believe that the proposed ferritin-nanocage-based multivalent vaccine platform will provide strong protection against emerging SARS-CoV-2 variants of concern (VOCs).
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7

Kim, Seong A., Yeram Lee, Yeju Ko, Seohyun Kim, Gi Beom Kim, Na Kyeong Lee, Wonkyung Ahn, et al. "Protein-based nanocages for vaccine development." Journal of Controlled Release 353 (January 2023): 767–91. http://dx.doi.org/10.1016/j.jconrel.2022.12.022.

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8

Schoonen, Lise, and Jan C. M. van Hest. "Functionalization of protein-based nanocages for drug delivery applications." Nanoscale 6, no. 13 (2014): 7124–41. http://dx.doi.org/10.1039/c4nr00915k.

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9

Kalathiya, Umesh, Monikaben Padariya, Robin Fahraeus, Soumyananda Chakraborti, and Ted R. Hupp. "Multivalent Display of SARS-CoV-2 Spike (RBD Domain) of COVID-19 to Nanomaterial, Protein Ferritin Nanocages." Biomolecules 11, no. 2 (February 17, 2021): 297. http://dx.doi.org/10.3390/biom11020297.

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SARS-CoV-2, or COVID-19, has a devastating effect on our society, both in terms of quality of life and death rates; hence, there is an urgent need for developing safe and effective therapeutics against SARS-CoV-2. The most promising strategy to fight against this deadly virus is to develop an effective vaccine. Internalization of SARS-CoV-2 into the human host cell mainly occurs through the binding of the coronavirus spike protein (a trimeric surface glycoprotein) to the human angiotensin-converting enzyme 2 (ACE2) receptor. The spike-ACE2 protein–protein interaction is mediated through the receptor-binding domain (RBD) of the spike protein. Mutations in the spike RBD can significantly alter interactions with the ACE2 host receptor. Due to its important role in virus transmission, the spike RBD is considered to be one of the key molecular targets for vaccine development. In this study, a spike RBD-based subunit vaccine was designed by utilizing a ferritin protein nanocage as a scaffold. Several fusion protein constructs were designed in silico by connecting the spike RBD via a synthetic linker (different sizes) to different ferritin subunits (H-ferritin and L-ferritin). The stability and the dynamics of the engineered nanocage constructs were tested by extensive molecular dynamics simulation (MDS). Based on our MDS analysis, a five amino acid-based short linker (S-Linker) was the most effective for displaying the spike RBD over the surface of ferritin. The behavior of the spike RBD binding regions from the designed chimeric nanocages with the ACE2 receptor was highlighted. These data propose an effective multivalent synthetic nanocage, which might form the basis for new vaccine therapeutics designed against viruses such as SARS-CoV-2.
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10

Palombarini, Federica, Elisa Di Fabio, Alberto Boffi, Alberto Macone, and Alessandra Bonamore. "Ferritin Nanocages for Protein Delivery to Tumor Cells." Molecules 25, no. 4 (February 13, 2020): 825. http://dx.doi.org/10.3390/molecules25040825.

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The delivery of therapeutic proteins is one of the greatest challenges in the treatment of human diseases. In this frame, ferritins occupy a very special place. Thanks to their hollow spherical structure, they are used as modular nanocages for the delivery of anticancer drugs. More recently, the possibility of encapsulating even small proteins with enzymatic or cytotoxic activity is emerging. Among all ferritins, particular interest is paid to the Archaeoglobus fulgidus one, due to its peculiar ability to associate/dissociate in physiological conditions. This protein has also been engineered to allow recognition of human receptors and used in vitro for the delivery of cytotoxic proteins with extremely promising results.
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11

Ren, Huimei, Shaozhou Zhu, and Guojun Zheng. "Nanoreactor Design Based on Self-Assembling Protein Nanocages." International Journal of Molecular Sciences 20, no. 3 (January 30, 2019): 592. http://dx.doi.org/10.3390/ijms20030592.

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Self-assembling proteins that form diverse architectures are widely used in material science and nanobiotechnology. One class belongs to protein nanocages, which are compartments with nanosized internal spaces. Because of the precise nanoscale structures, proteinaceous compartments are ideal materials for use as general platforms to create distinct microenvironments within confined cellular environments. This spatial organization strategy brings several advantages including the protection of catalyst cargo, faster turnover rates, and avoiding side reactions. Inspired by diverse molecular machines in nature, bioengineers have developed a variety of self-assembling supramolecular protein cages for use as biosynthetic nanoreactors that mimic natural systems. In this mini-review, we summarize current progress and ongoing efforts creating self-assembling protein based nanoreactors and their use in biocatalysis and synthetic biology. We also highlight the prospects for future research on these versatile nanomaterials.
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12

Almeida, Ana V., Ana J. Carvalho, and Alice S. Pereira. "Encapsulin nanocages: Protein encapsulation and iron sequestration." Coordination Chemistry Reviews 448 (December 2021): 214188. http://dx.doi.org/10.1016/j.ccr.2021.214188.

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13

Theil, Elizabeth C., Manolis Matzapetakis, and Xiaofeng Liu. "Ferritins: iron/oxygen biominerals in protein nanocages." JBIC Journal of Biological Inorganic Chemistry 11, no. 7 (July 26, 2006): 803–10. http://dx.doi.org/10.1007/s00775-006-0125-6.

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14

Diaz, D., A. Care, and A. Sunna. "Engineering protein nanocages for targeted photodynamic therapy." New Biotechnology 44 (October 2018): S10. http://dx.doi.org/10.1016/j.nbt.2018.05.171.

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15

Guan, Xingang, Yu Chang, Jinghui Sun, Jianxi Song, and Yu Xie. "Engineered Hsp Protein Nanocages for siRNA Delivery." Macromolecular Bioscience 18, no. 5 (April 17, 2018): 1800013. http://dx.doi.org/10.1002/mabi.201800013.

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16

Zhang, Xiaorong, Tuo Zhang, Yingjie Wang, Yu Liu, Jiachen Zang, and Guanghua Zhao. "Reversible structure transformation between protein nanocages and nanorods controlled by small molecules." Chemical Communications 57, no. 96 (2021): 12996–99. http://dx.doi.org/10.1039/d1cc04510e.

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17

Jin, Yiliang, Jiuyang He, Kelong Fan, and Xiyun Yan. "Ferritin variants: inspirations for rationally designing protein nanocarriers." Nanoscale 11, no. 26 (2019): 12449–59. http://dx.doi.org/10.1039/c9nr03823j.

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Ferritin is endowed with a unique structure and the ability to self-assemble. Besides, genetic manipulation can easily tune the structure and functions of ferritin nanocages, which further expands the biomedical applications of ferritin.
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18

Villegas, José A., Nairiti J. Sinha, Naozumi Teramoto, Christopher D. Von Bargen, Darrin J. Pochan, and Jeffery G. Saven. "Computational Design of Single-Peptide Nanocages with Nanoparticle Templating." Molecules 27, no. 4 (February 12, 2022): 1237. http://dx.doi.org/10.3390/molecules27041237.

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Protein complexes perform a diversity of functions in natural biological systems. While computational protein design has enabled the development of symmetric protein complexes with spherical shapes and hollow interiors, the individual subunits often comprise large proteins. Peptides have also been applied to self-assembly, and it is of interest to explore such short sequences as building blocks of large, designed complexes. Coiled-coil peptides are promising subunits as they have a symmetric structure that can undergo further assembly. Here, an α-helical 29-residue peptide that forms a tetrameric coiled coil was computationally designed to assemble into a spherical cage that is approximately 9 nm in diameter and presents an interior cavity. The assembly comprises 48 copies of the designed peptide sequence. The design strategy allowed breaking the side chain conformational symmetry within the peptide dimer that formed the building block (asymmetric unit) of the cage. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) techniques showed that one of the seven designed peptide candidates assembled into individual nanocages of the size and shape. The stability of assembled nanocages was found to be sensitive to the assembly pathway and final solution conditions (pH and ionic strength). The nanocages templated the growth of size-specific Au nanoparticles. The computational design serves to illustrate the possibility of designing target assemblies with pre-determined specific dimensions using short, modular coiled-coil forming peptide sequences.
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19

Lv, Chenyan, Xiaorong Zhang, Yu Liu, Tuo Zhang, Hai Chen, Jiachen Zang, Bowen Zheng, and Guanghua Zhao. "Redesign of protein nanocages: the way from 0D, 1D, 2D to 3D assembly." Chemical Society Reviews 50, no. 6 (2021): 3957–89. http://dx.doi.org/10.1039/d0cs01349h.

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20

Unida, Valeria, Giulia Vindigni, Sofia Raniolo, Carmine Stolfi, Alessandro Desideri, and Silvia Biocca. "Folate-Functionalization Enhances Cytotoxicity of Multivalent DNA Nanocages on Triple-Negative Breast Cancer Cells." Pharmaceutics 14, no. 12 (November 26, 2022): 2610. http://dx.doi.org/10.3390/pharmaceutics14122610.

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DNA is an excellent programmable polymer for the generation of self-assembled multivalent nanostructures useful for biomedical applications. Herein, we developed (i) folate-functionalized nanocages (Fol-NC), very efficiently internalized by tumor cells overexpressing the α isoform of the folate receptor; (ii) AS1411-linked nanocages (Apt-NC), internalized through nucleolin, a protein overexpressed in the cell surface of many types of cancers; and (iii) nanostructures that harbor both folate and AS1411 aptamer functionalization (Fol-Apt-NC). We analyzed the specific miRNA silencing activity of all types of nanostructures harboring miRNA sequestering sequences complementary to miR-21 and the cytotoxic effect when loaded with doxorubicin in a drug-resistant triple-negative breast cancer cell line. We demonstrate that the presence of folate as a targeting ligand increases the efficiency in miR-21 silencing compared to nanocages functionalized with AS1411. Double-functionalized nanocages (Fol-Apt-NC), loaded with doxorubicin, resulted in an increase of over 51% of the cytotoxic effect on MDA-MB-231 cells compared to free doxorubicin, demonstrating, besides selectivity, the ability of nanocages to overcome Dox chemoresistance. The higher efficiency of the folate-functionalized nanocages is due to the way of entrance, which induces more than four times higher intracellular stability and indicates that the folate-mediated route of cell entry is more efficient than the nucleolin-mediated one when both folate and AS1411 modifications are present.
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21

Chen, H., K. Zhou, Y. Wang, J. Zang, and G. Zhao. "Self-assembly of engineered protein nanocages into reversible ordered 3D superlattices mediated by zinc ions." Chemical Communications 55, no. 75 (2019): 11299–302. http://dx.doi.org/10.1039/c9cc06262a.

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22

Huang, Haiqin, Shirui Yuan, Zhuo Ma, Peng Ji, Xiaonan Ma, Zhenghong Wu, and Xiaole Qi. "Genetic recombination of poly(l-lysine) functionalized apoferritin nanocages that resemble viral capsid nanometer-sized platforms for gene therapy." Biomaterials Science 8, no. 6 (2020): 1759–70. http://dx.doi.org/10.1039/c9bm01822k.

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23

Bhaskar, Sathyamoorthy, and Sierin Lim. "Engineering protein nanocages as carriers for biomedical applications." NPG Asia Materials 9, no. 4 (April 2017): e371-e371. http://dx.doi.org/10.1038/am.2016.128.

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24

Almeida, Ana V., Ana J. Carvalho, Tomás Calmeiro, Nykola C. Jones, Søren V. Hoffmann, Elvira Fortunato, Alice S. Pereira, and Pedro Tavares. "Condensation and Protection of DNA by the Myxococcus xanthus Encapsulin: A Novel Function." International Journal of Molecular Sciences 23, no. 14 (July 15, 2022): 7829. http://dx.doi.org/10.3390/ijms23147829.

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Encapsulins are protein nanocages capable of harboring smaller proteins (cargo proteins) within their cavity. The function of the encapsulin systems is related to the encapsulated cargo proteins. The Myxococcus xanthus encapsulin (EncA) naturally encapsulates ferritin-like proteins EncB and EncC as cargo, resulting in a large iron storage nanocompartment, able to accommodate up to 30,000 iron atoms per shell. In the present manuscript we describe the binding and protection of circular double stranded DNA (pUC19) by EncA using electrophoretic mobility shift assays (EMSA), atomic force microscopy (AFM), and DNase protection assays. EncA binds pUC19 with an apparent dissociation constant of 0.3 ± 0.1 µM and a Hill coefficient of 1.4 ± 0.1, while EncC alone showed no interaction with DNA. Accordingly, the EncAC complex displayed a similar DNA binding capacity as the EncA protein. The data suggest that initially, EncA converts the plasmid DNA from a supercoiled to a more relaxed form with a beads-on-a-string morphology. At higher concentrations, EncA self-aggregates, condensing the DNA. This process physically protects DNA from enzymatic digestion by DNase I. The secondary structure and thermal stability of EncA and the EncA−pUC19 complex were evaluated using synchrotron radiation circular dichroism (SRCD) spectroscopy. The overall secondary structure of EncA is maintained upon interaction with pUC19 while the melting temperature of the protein (Tm) slightly increased from 76 ± 1 °C to 79 ± 1 °C. Our work reports, for the first time, the in vitro capacity of an encapsulin shell to interact and protect plasmid DNA similarly to other protein nanocages that may be relevant in vivo.
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Huang, Xinglu, Jane Chisholm, Jie Zhuang, Yanyu Xiao, Gregg Duncan, Xiaoyuan Chen, Jung Soo Suk, and Justin Hanes. "Protein nanocages that penetrate airway mucus and tumor tissue." Proceedings of the National Academy of Sciences 114, no. 32 (July 24, 2017): E6595—E6602. http://dx.doi.org/10.1073/pnas.1705407114.

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Reports on drug delivery systems capable of overcoming multiple biological barriers are rare. We introduce a nanoparticle-based drug delivery technology capable of rapidly penetrating both lung tumor tissue and the mucus layer that protects airway tissues from nanoscale objects. Specifically, human ferritin heavy-chain nanocages (FTn) were functionalized with polyethylene glycol (PEG) in a unique manner that allows robust control over PEG location (nanoparticle surface only) and surface density. We varied PEG surface density and molecular weight to discover PEGylated FTn that rapidly penetrated both mucus barriers and tumor tissues in vitro and in vivo. Upon inhalation in mice, PEGylated FTn with optimized PEGylation rapidly penetrated the mucus gel layer and thus provided a uniform distribution throughout the airways. Subsequently, PEGylated FTn preferentially penetrated and distributed within orthotopic lung tumor tissue, and selectively entered cancer cells, in a transferrin receptor 1-dependent manner, which is up-regulated in most cancers. To test the potential therapeutic benefits, doxorubicin (DOX) was conjugated to PEGylated FTn via an acid-labile linker to facilitate intracellular release of DOX after cell entry. Inhalation of DOX-loaded PEGylated FTn led to 60% survival, compared with 10% survival in the group that inhaled DOX in solution at the maximally tolerated dose, in a murine model of malignant airway lung cancer. This approach may provide benefits as an adjuvant therapy combined with systemic chemo- or immunotherapy or as a stand-alone therapy for patients with tumors confined to the airways.
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Theil, Elizabeth C., Takehiko Tosha, and Rabindra K. Behera. "Solving Biology’s Iron Chemistry Problem with Ferritin Protein Nanocages." Accounts of Chemical Research 49, no. 5 (May 2, 2016): 784–91. http://dx.doi.org/10.1021/ar500469e.

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27

Beck, Tobias, Stephan Tetter, Matthias Künzle, and Donald Hilvert. "Construction of Matryoshka-Type Structures from Supercharged Protein Nanocages." Angewandte Chemie 127, no. 3 (November 13, 2014): 951–54. http://dx.doi.org/10.1002/ange.201408677.

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Beck, Tobias, Stephan Tetter, Matthias Künzle, and Donald Hilvert. "Construction of Matryoshka-Type Structures from Supercharged Protein Nanocages." Angewandte Chemie International Edition 54, no. 3 (November 13, 2014): 937–40. http://dx.doi.org/10.1002/anie.201408677.

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29

Divine, Robby, Ha V. Dang, George Ueda, Jorge A. Fallas, Ivan Vulovic, William Sheffler, Shally Saini, et al. "Designed proteins assemble antibodies into modular nanocages." Science 372, no. 6537 (April 1, 2021): eabd9994. http://dx.doi.org/10.1126/science.abd9994.

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Multivalent display of receptor-engaging antibodies or ligands can enhance their activity. Instead of achieving multivalency by attachment to preexisting scaffolds, here we unite form and function by the computational design of nanocages in which one structural component is an antibody or Fc-ligand fusion and the second is a designed antibody-binding homo-oligomer that drives nanocage assembly. Structures of eight nanocages determined by electron microscopy spanning dihedral, tetrahedral, octahedral, and icosahedral architectures with 2, 6, 12, and 30 antibodies per nanocage, respectively, closely match the corresponding computational models. Antibody nanocages targeting cell surface receptors enhance signaling compared with free antibodies or Fc-fusions in death receptor 5 (DR5)–mediated apoptosis, angiopoietin-1 receptor (Tie2)–mediated angiogenesis, CD40 activation, and T cell proliferation. Nanocage assembly also increases severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pseudovirus neutralization by α-SARS-CoV-2 monoclonal antibodies and Fc–angiotensin-converting enzyme 2 (ACE2) fusion proteins.
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Mainini, Francesco, Arianna Bonizzi, Marta Sevieri, Leopoldo Sitia, Marta Truffi, Fabio Corsi, and Serena Mazzucchelli. "Protein-Based Nanoparticles for the Imaging and Treatment of Solid Tumors: The Case of Ferritin Nanocages, a Narrative Review." Pharmaceutics 13, no. 12 (November 25, 2021): 2000. http://dx.doi.org/10.3390/pharmaceutics13122000.

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Protein nanocages have been studied extensively, due to their unique architecture, exceptional biocompatibility and highly customization capabilities. In particular, ferritin nanocages (FNs) have been employed for the delivery of a vast array of molecules, ranging from chemotherapeutics to imaging agents, among others. One of the main favorable characteristics of FNs is their intrinsic targeting efficiency toward the Transferrin Receptor 1, which is overexpressed in many tumors. Furthermore, genetic manipulation can be employed to introduce novel variants that are able to improve the loading capacity, targeting capabilities and bio-availability of this versatile drug delivery system. In this review, we discuss the main characteristics of FN and the most recent applications of this promising nanotechnology in the field of oncology with a particular emphasis on the imaging and treatment of solid tumors.
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Wang, Yingjie, Hai Chen, Jiachen Zang, Xiuqing Zhang, and Guanghua Zhao. "Re-designing ferritin nanocages for mercuric ion detection." Analyst 144, no. 19 (2019): 5890–97. http://dx.doi.org/10.1039/c9an01110b.

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To extend the applications of protein nanocages, we explored human H-chain ferritin as a platform for Hg2+ detection by combining the ability of newly fabricated ferritin mutant to bind to Hg2+ with high affinity and the fluorescence of dyes quenched by graphene oxide.
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Boyton, India, Sophia C. Goodchild, Dennis Diaz, Aaron Elbourne, Lyndsey E. Collins-Praino, and Andrew Care. "Characterizing the Dynamic Disassembly/Reassembly Mechanisms of Encapsulin Protein Nanocages." ACS Omega 7, no. 1 (December 20, 2021): 823–36. http://dx.doi.org/10.1021/acsomega.1c05472.

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Beck, Tobias. "Engineering of protein nanocages for superlatttice formation and nanoparticle encapsulation." Acta Crystallographica Section A Foundations and Advances 77, a2 (August 14, 2021): C925. http://dx.doi.org/10.1107/s0108767321087742.

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Zhou, K., H. Chen, S. Zhang, Y. Wang, and G. Zhao. "Disulfide-mediated reversible two-dimensional self-assembly of protein nanocages." Chemical Communications 55, no. 52 (2019): 7510–13. http://dx.doi.org/10.1039/c9cc03085a.

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Cornell, Thomas A., Jing Fu, Stephanie H. Newland, and Brendan P. Orner. "Detection of Specific Protein–Protein Interactions in Nanocages by Engineering Bipartite FlAsH Binding Sites." Journal of the American Chemical Society 135, no. 44 (October 28, 2013): 16618–24. http://dx.doi.org/10.1021/ja4085034.

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36

Bolis, Dimos, Anastasia S. Politou, Geoff Kelly, Annalisa Pastore, and Piero Andrea Temussi. "Protein Stability in Nanocages: A Novel Approach for Influencing Protein Stability by Molecular Confinement." Journal of Molecular Biology 336, no. 1 (February 2004): 203–12. http://dx.doi.org/10.1016/j.jmb.2003.11.056.

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37

Cho, Eunji, Gi-Hoon Nam, Yeonsun Hong, Yoon Kyoung Kim, Dong-Hwee Kim, Yoosoo Yang, and In-San Kim. "Comparison of exosomes and ferritin protein nanocages for the delivery of membrane protein therapeutics." Journal of Controlled Release 279 (June 2018): 326–35. http://dx.doi.org/10.1016/j.jconrel.2018.04.037.

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Zhao, Jianmin, Ting Zheng, Jiaxi Gao, Shijing Guo, Xingxing Zhou, and Wenju Xu. "A sub-picomolar assay for protein by using cubic Cu2O nanocages loaded with Au nanoparticles as robust redox probes and efficient non-enzymatic electrocatalysts." Analyst 142, no. 5 (2017): 794–99. http://dx.doi.org/10.1039/c6an02599d.

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In this work, a simple and sensitive electrochemical aptasensor for protein (thrombin – TB used as the model) was developed by using cubic Cu2O nanocages (Cu2O-NCs) loaded with Au nanoparticles (AuNPs@Cu2O-NCs) as non-enzymatic electrocatalysts and robust redox probes.
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Zhang, Xiaorong, Jiachen Zang, Hai Chen, Kai Zhou, Tuo Zhang, Chenyan Lv, and Guanghua Zhao. "Thermostability of protein nanocages: the effect of natural extra peptide on the exterior surface." RSC Advances 9, no. 43 (2019): 24777–82. http://dx.doi.org/10.1039/c9ra04785a.

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Sitia, Leopoldo, Arianna Bonizzi, Serena Mazzucchelli, Sara Negri, Cristina Sottani, Elena Grignani, Maria Antonietta Rizzuto, et al. "Selective Targeting of Cancer-Associated Fibroblasts by Engineered H-Ferritin Nanocages Loaded with Navitoclax." Cells 10, no. 2 (February 5, 2021): 328. http://dx.doi.org/10.3390/cells10020328.

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Cancer-associated fibroblasts (CAFs) are key actors in regulating cancer progression. They promote tumor growth, metastasis formation, and induce drug resistance. For these reasons, they are emerging as potential therapeutic targets. Here, with the aim of developing CAF-targeted drug delivery agents, we functionalized H-ferritin (HFn) nanocages with fibroblast activation protein (FAP) antibody fragments. Functionalized nanocages (HFn-FAP) have significantly higher binding with FAP+ CAFs than with FAP− cancer cells. We loaded HFn-FAP with navitoclax (Nav), an experimental Bcl-2 inhibitor pro-apoptotic drug, whose clinical development is limited by its strong hydrophobicity and toxicity. We showed that Nav is efficiently loaded into HFn (HNav), maintaining its mechanism of action. Incubating Nav-loaded functionalized nanocages (HNav-FAP) with FAP+ cells, we found significantly higher cytotoxicity as compared to non-functionalized HNav. This was correlated with a significantly higher drug release only in FAP+ cells, confirming the specific targeting ability of functionalized HFn. Finally, we showed that HFn-FAP is able to reach the tumor and to target CAFs in a mouse syngeneic model of triple negative breast cancer after intravenous administration. Our data show that HNav-FAP could be a promising tool to enhance specific drug delivery into CAFs, thus opening new therapeutic possibilities focused on tumor microenvironment.
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41

van der Put, Robert M. F., Bernard Metz, and Roland J. Pieters. "Carriers and Antigens: New Developments in Glycoconjugate Vaccines." Vaccines 11, no. 2 (January 19, 2023): 219. http://dx.doi.org/10.3390/vaccines11020219.

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Glycoconjugate vaccines have proven their worth in the protection and prevention of infectious diseases. The introduction of the Haemophilus influenzae type b vaccine is the prime example, followed by other glycoconjugate vaccines. Glycoconjugate vaccines consist of two components: the carrier protein and the carbohydrate antigen. Current carrier proteins are tetanus toxoid, diphtheria toxoid, CRM197, Haemophilus protein D and the outer membrane protein complex of serogroup B meningococcus. Carbohydrate antigens have been produced mainly by extraction and purification from the original host. However, current efforts show great advances in the development of synthetically produced oligosaccharides and bioconjugation. This review evaluates the advances of glycoconjugate vaccines in the last five years. We focus on developments regarding both new carriers and antigens. Innovative developments regarding carriers are outer membrane vesicles, glycoengineered proteins, new carrier proteins, virus-like particles, protein nanocages and peptides. With regard to conjugated antigens, we describe recent developments in the field of antimicrobial resistance (AMR) and ESKAPE pathogens.
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Bhaskar, Sathyamoorthy, Steven Thng, and Sierin Lim. "Engineered Protein Nanocages for Targeted and Enhanced Dermal Melanocyte Cellular Uptake." Advanced NanoBiomed Research 1, no. 7 (May 5, 2021): 2000115. http://dx.doi.org/10.1002/anbr.202000115.

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Ghisaidoobe, Amar BT, and Sang J. Chung. "Functionalized protein nanocages as a platform of targeted therapy and immunodetection." Nanomedicine 10, no. 24 (December 2015): 3579–95. http://dx.doi.org/10.2217/nnm.15.175.

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Corsi, Fabio, and Serena Mazzucchelli. "The potential of protein-based nanocages for imaging and drug delivery." Therapeutic Delivery 7, no. 3 (March 2016): 149–51. http://dx.doi.org/10.4155/tde.15.95.

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Nasu, Erika, Norifumi Kawakami, and Kenji Miyamoto. "Nanopore-Controlled Dual-Surface Modifications on Artificial Protein Nanocages as Nanocarriers." ACS Applied Nano Materials 4, no. 3 (March 2, 2021): 2434–39. http://dx.doi.org/10.1021/acsanm.0c02972.

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Li, Xiao, Yajie Zhang, Hong Chen, Jian Sun, and Fude Feng. "Protein Nanocages for Delivery and Release of Luminescent Ruthenium(II) Polypyridyl Complexes." ACS Applied Materials & Interfaces 8, no. 35 (August 25, 2016): 22756–61. http://dx.doi.org/10.1021/acsami.6b07038.

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Huang, Xinglu, Jie Zhuang, Seung Woo Chung, Buwei Huang, Gilad Halpert, Karina Negron, Xuanrong Sun, et al. "Hypoxia-tropic Protein Nanocages for Modulation of Tumor- and Chemotherapy-Associated Hypoxia." ACS Nano 13, no. 1 (December 21, 2018): 236–47. http://dx.doi.org/10.1021/acsnano.8b05399.

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Luo, Yanan, Xuenv Wang, Dan Du, and Yuehe Lin. "Hyaluronic acid-conjugated apoferritin nanocages for lung cancer targeted drug delivery." Biomaterials Science 3, no. 10 (2015): 1386–94. http://dx.doi.org/10.1039/c5bm00067j.

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Yan, Fei, Yan Zhang, Kyu S. Kim, Hsiang-Kuo Yuan, and Tuan Vo-Dinh. "Cellular Uptake and Photodynamic Activity of Protein Nanocages Containing Methylene Blue Photosensitizing Drug." Photochemistry and Photobiology 86, no. 3 (January 27, 2010): 662–66. http://dx.doi.org/10.1111/j.1751-1097.2009.00696.x.

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Patterson, Dustin P., Min Su, Titus M. Franzmann, Aaron Sciore, Georgios Skiniotis, and E. Neil G. Marsh. "Characterization of a highly flexible self-assembling protein system designed to form nanocages." Protein Science 23, no. 2 (December 16, 2013): 190–99. http://dx.doi.org/10.1002/pro.2405.

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