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1.
Int J Biol Macromol ; 191: 152-160, 2021 Sep 20.
Artigo em Inglês | MEDLINE | ID: mdl-34547309

RESUMO

The favorable physicochemical properties are essential for the application of protein-based nanovehicles in the field of biomaterials. Herein, we found that the thermal stability of Marsupenaeus japonicus ferritin (MjFer) (Tm = 109.1 ± 0.4 °C) is markedly higher than human H-chain ferritin (HuHF) (Tm = 87.7 ± 0.3 °C), although they share a high structural similarity. Multiple results indicated that the promoted thermal stability of MjFer is mainly derived from the salt bridges located at the C3 interface. Consequently, MjFer exhibits strong protective effects on encapsulated curcumin upon exposure at high temperatures. In contrast, most of the curcumin loaded HuHF composites precipitated rapidly under the same conditions. These findings elucidated the molecular mechanism of the hyperthermostability of MjFer and illustrated that MjFer could act as a robust insulation nanocarrier for bioactive compounds against various thermal treatments.

2.
Crit Rev Food Sci Nutr ; : 1-16, 2021 Aug 12.
Artigo em Inglês | MEDLINE | ID: mdl-34382897

RESUMO

As the second most abundant trace element in the human body, zinc nutrition is constantly a hot topic. More than one-third population is suffering zinc deficiency, which results in various types of diseases or nutritional deficiencies. Traditional ways of zinc supplementation seem with low absorption rates and significant side effects. Zinc supplements with dietary components are easily accessible and improve zinc utilization rate significantly. Also, mechanisms of maintaining zinc homeostasis are of broad interest. The present review focuses on zinc nutrition in human health in inductive methods. Mainly elaborate on different diseases relating to zinc disorder, highlighting the impact on the immune system and the recent COVID-19. Then raise food-derived zinc-binding compounds, including protein, peptide, polysaccharide, and polyphenol, and also analyze their possibilities to serve as zinc complementary. Finally, illustrate the way to maintain zinc homeostasis and the corresponding mechanisms. The review provides data information for maintaining zinc homeostasis with the food-derived matrix.

3.
Nat Commun ; 12(1): 4849, 2021 08 11.
Artigo em Inglês | MEDLINE | ID: mdl-34381032

RESUMO

Although various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored. Here, we describe an approach to realize the self-assembly transformation of dimeric building blocks by adjusting their geometric arrangement. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimer; twelve of these dimers interact with each other in a head-to-side manner to generate 24-meric hollow protein nanocage in the presence of Ca2+ or PEG. By tuning two contiguous dimeric proteins to interact in a fully or partially side-by-side fashion through protein interface redesign, we can render the self-assembly transformation of such dimeric building blocks from the protein nanocage to filament, nanorod and nanoribbon in response to multiple external stimuli. We show similar dimeric protein building blocks can generate three kinds of protein materials in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.


Assuntos
Nanoestruturas/química , Proteínas/química , Cálcio/química , Ferritinas/química , Nanoestruturas/ultraestrutura , Nanotecnologia , Polietilenoglicóis/química , Multimerização Proteica , Thermotoga maritima
4.
Int J Mol Sci ; 22(15)2021 Jul 23.
Artigo em Inglês | MEDLINE | ID: mdl-34360624

RESUMO

Although apoferritin has been widely utilized as a new class of natural protein nanovehicles for encapsulation and delivery of nutraceuticals, its ability to remove metal heavy ions has yet to be explored. In this study, for the first time, we demonstrated that the ferritin from kuruma prawns (Marsupenaeus japonicus), named MjF, has a pronouncedly larger ability to resist denaturation induced by Cd2+ and Hg2+ as compared to its analogue, human H-chain ferritin (HuHF), despite the fact that these two proteins share a high similarity in protein structure. Treatment of HuHF with Cd2+ or Hg2+ at a metal ion/protein shell ratio of 100/1 resulted in marked protein aggregation, while the MjF solution was kept constantly clear upon treatment with Cd2+ and Hg2+ at different protein shell/metal ion ratios (50/1, 100/1, 250/1, 500/1, 1000/1, and 2500/1). Structural comparison analyses in conjunction with the newly solved crystal structure of the complex of MjF plus Cd2+ or Hg2+ revealed that cysteine (Cys) is a major residue responsible for such binding, and that the large difference in the ability to resist denaturation induced by these two heavy metal ions between MjF and HuHF is mainly derived from the different positions of Cys residues in these two proteins; namely, Cys residues in HuHF are located on the outer surface, while Cys residues from MjF are buried within the protein shell. All of these findings raise the high possibility that prawn ferritin, as a food-derived protein, could be developed into a novel bio-template to remove heavy metal ions from contaminated food systems.


Assuntos
Cádmio/química , Ferritinas/química , Mercúrio/química , Metais Pesados/química , Penaeidae/química , Animais
5.
J Agric Food Chem ; 69(36): 10669-10677, 2021 Sep 15.
Artigo em Inglês | MEDLINE | ID: mdl-34463093

RESUMO

Chloroquine (CQ) is a famous medicine for treatment of diseases including malaria and pneumonia caused by COVID-19, but gastrointestinal disorder caused by its oral administration is a great concern. Milk is usually recommended to be taken with CQ to reduce such effect. However, the mechanism underlying this phenomenon remains unknown. Here, we found that ß-lactoglobulin (ß-LG), α-lactalbumin (α-LA), bovine serum albumin (BSA), and lactoferrin (LF) in whey proteins were able to interact with CQ to form complexes as suggested by fluorescence resonance energy transfer (FRET) and molecular docking. Indeed, the crystal structure revealed that ß-LG is bound to CQ through hydrophobic interactions and hydrogen bonding with a ratio of 1:1. Consequently, the formation of these protein-CQ complexes not only reduced the cytotoxicity of chloroquine to the stomach and gut cells but also facilitated its uptake by cells. This work gave an example to understand the relationship between food and drug.


Assuntos
COVID-19 , Cloroquina , COVID-19/tratamento farmacológico , Cloroquina/farmacologia , Humanos , Lactalbumina , Lactoglobulinas , Proteínas do Leite , Simulação de Acoplamento Molecular , SARS-CoV-2 , Proteínas do Soro do Leite
6.
J Agric Food Chem ; 69(30): 8482-8491, 2021 Aug 04.
Artigo em Inglês | MEDLINE | ID: mdl-34286590

RESUMO

Improving the stability and bioavailability of catechins is of great importance. Epigallocatechin (EGC), the major catechin in green tea, is a potent antioxidant with numerous attributed health benefits. However, the low permeability and stability limit its enrichment in the diet for preventive medicine. In this study, we explored the interaction of EGC and α-lactalbumin by spectroscopic, thermodynamic, and crystallographic methods. The isothermal titration calorimetry experiments elucidated that α-lactalbumin binds to EGC at a ratio of 1:1 with a low affinity of (4.01 ± 0.11) × 105 M-1. A crystal structure solved at a high resolution (1.2 Å) provided direct evidence for the weak interaction between EGC and α-lactalbumin at an atomic level. The novel binding site was discovered at the exterior surface of α-lactalbumin for the first time, supporting a new binding behavior. Consequently, our results demonstrated that the binding of α-lactalbumin to EGC could protect EGC against light-induced, thermal-induced, and pH-induced damage. More importantly, the formed complex has better bioaccessibility than unbound EGC, which was approved by a cell absorption experiment. Such research is beneficial for designing protein-based nanocarriers for polyphenols.


Assuntos
Catequina , Células CACO-2 , Catequina/análogos & derivados , Catequina/análise , Humanos , Lactalbumina , Chá
7.
Crit Rev Food Sci Nutr ; : 1-12, 2021 Apr 16.
Artigo em Inglês | MEDLINE | ID: mdl-33860692

RESUMO

Ferritin is an important iron storage protein, which is widely existed in all forms of life. Ferritin can regulate iron homeostasis when iron ions are lacking or enriched in the body, so as to avoid iron deficiency diseases and iron poisoning. Ferritin presents a hollow nanocage, which can store ions or other small molecular substances in the cavity. Therefore, ferritin shows its potential as a functional nanomaterial that can deliver nutrients or drugs in a targeted manner to improve bioavailability. Due to the special structure, the research on ferritin has attracted more and more attention in recent years. In this paper, the structural characteristics of ferritin were introduced, and the natural purification and prokaryotic expression methods of ferritin from different sources were described. At the same time, ferritin can bind to small molecules, so that it has the activity of small molecules, to construct a new type of ferritin. As a result, ferritin plays an important role as a nutrient substance, in targeted transport, and disease monitoring, etc. In conclusion, the yield of ferritin can be improved by means of molecular biology. Meanwhile, molecular modification can be used to make ferritin have unique activity and function, which lays a foundation for subsequent research. HighlightsThe molecular and structural properties of ferritins were clearly described.Isolation and purification technologies of ferritin were compared.Characterization, functions and molecular modifications mechanism of ferritin were reviewed.The applications of ferritin in pharmaceutical and food industry were prospected.

8.
Chem Soc Rev ; 50(6): 3957-3989, 2021 Mar 21.
Artigo em Inglês | MEDLINE | ID: mdl-33587075

RESUMO

Compartmentalization is a hallmark of living systems. Through compartmentalization, ubiquitous protein nanocages such as viral capsids, ferritin, small heat shock proteins, and DNA-binding proteins from starved cells fulfill a variety of functions, while their shell-like structures hold great promise for various applications in the field of nanomedicine and nanotechnology. However, the number and structure of natural protein nanocages are limited, and these natural protein nanocages may not be suited for a given application, which might impede their further application as nanovehicles, biotemplates or building blocks. To overcome these shortcomings, different strategies have been developed by scientists to construct artificial protein nanocages, and 1D, 2D and 3D protein arrays with protein nanocages as building blocks through genetic and chemical modification to rival the size and functionality of natural protein nanocages. This review outlines the recent advances in the field of the design and construction of artificial protein nanocages and their assemblies with higher order, summarizes the strategies for creating the assembly of protein nanocages from zero-dimension to three dimensions, and introduces their corresponding applications in the preparation of nanomaterials, electrochemistry, and drug delivery. The review will highlight the roles of both the inter-subunit/intermolecular interactions at the key interface and the protein symmetry in constructing and controlling protein nanocage assemblies with different dimensions.


Assuntos
Nanoestruturas/química , Proteínas/química , Proteínas do Capsídeo/química , Catálise , Complexos de Coordenação/química , Portadores de Fármacos/química , Ferritinas/química , Propriedades de Superfície
9.
Food Chem ; 346: 128879, 2021 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-33406454

RESUMO

Ferritin can be widely used as functional nanomaterial. But the physiological activity of ferritin can be damaged under excessive temperatures, which affect the self-assembly property. In this study, point mutation was produced in Asp120 to Gly120 of ferritin amino acid sequence and the heat resistance was improved significantly. The thermal denaturation temperature of mutated ferritin is 89.17 °C and has increased by 13 °C more than the wild-type oyster ferritin. The effect of thermal treatment on the denaturation, aggregation state, particle size and the structure of ferritin was not changed before 90 °C. The computational modeling and analysis indicated that mutated ferritin promotes the overall structural stability assembly via decreasing the interaction energies of 62 percent energies in 3-fold interface. Improving the thermal stability of oyster ferritin by point mutation enhances its applications as a food ingredient.


Assuntos
Crassostrea/metabolismo , Ferritinas/metabolismo , Temperatura Alta , Mutação Puntual , Alimentos Marinhos/análise , Sequência de Aminoácidos , Animais , Crassostrea/química
10.
Food Chem ; 314: 126210, 2020 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-31972409

RESUMO

The unique nanocage structure of ferritin can be used as functional nanomaterials and has wide application prospects. However, thermal treatment may affect the structure of ferritin, further affecting self-assembly property. In this study, the oyster ferritin gene GF1 was obtained, prokaryotically expressed in E. coli BL21 (DE3). Then the purified ferritin was heated from 60 to 100 °C for 10 min with untreated ferritin as a control sample. The aggregation state of ferritin was investigated and the difference in protein structure was evaluated in terms of particle size and protein structures. The results of electrophoresis indicated that thermal treatment induced denaturation and aggregation of ferritin macromolecules. Moreover, the particle size distribution shifted to larger size trend and aggregates were visible with the heated samples and the secondary structure and tertiary structure were destroyed gradually. The findings are beneficial for understanding the relationship of the structure and function of ferritin.


Assuntos
Crassostrea/metabolismo , Ferritinas/metabolismo , Frutos do Mar/análise , Animais , Crassostrea/química , Ferritinas/química , Temperatura Alta , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína
11.
Analyst ; 144(19): 5890-5897, 2019 Sep 23.
Artigo em Inglês | MEDLINE | ID: mdl-31497803

RESUMO

Protein nanocages have recently received considerable attention in the fields of nanoscience and nanomedicine and have been used as either biotemplates for the preparation of a variety of nanomaterials or vehicles for drugs or imaging agents. However, their utilization for detection of heavy metal ions has yet to be explored. In this study, by grafting a mercury binding peptide (MBP) on the exterior surface of a recombinant human H-chain ferritin (rHuHF) nanocage, we successfully prepared a new protein nanocage (HuHF-MBP) which exhibits high binding capacity and affinity for Hg2+. The fluorescence of HuHF-MBP labeled with a green fluorescent dye fluorescein isothiocyanate (FITC) can be quenched by graphene oxide (GO), while addition of Hg2+ to the above solution recovered the quenched fluorescence in a dose-dependent manner. Thus, this system consisting of FITC-labeled HuHF-MBP and GO, where FITC and graphene oxide were used as fluorescent reporter probes, has great potential to be explored as a sensor for Hg2+ detection. Indeed, this newly constructed protein sensor exhibited high sensitivity and selectivity for Hg2+, and the limit of detection was 1.0 nM. The construction of this system provides an alternative strategy for the preparation of heavy metal ion sensors by using protein nanocages as biotemplates.

12.
J Nanobiotechnology ; 17(1): 79, 2019 Jul 05.
Artigo em Inglês | MEDLINE | ID: mdl-31277668

RESUMO

BACKGROUND: Protein nanocages have emerged as popular nanocarriers for either drug delivery or biotemplates for the preparation of nanomaterials. However, only three interfaces, namely exterior surface, intersubunit and inner cavity, have been used as reaction sites for the above purposes with all known protein nanocages. On the other hand, how to control the site of Au NCs formed within a targeted protein template while maintaining the functionality of protein itself remains challenging. RESULTS: In this work, inspired by compartmentalization in living systems, we firstly come up with the conception of "intrasubunit interfaces", located within subunit of protein nanocage. We built a new, specific compartment for fabrication of gold nanoclusters by genetic modification of the inherent ferroxidase center located within four-α-helix bundle of each ferritin subunit. This newly built compartment not only realizes the site-directed synthesis of gold nanoclusters but also has no effect on the functionality of ferritin itself such as encapsulation by its inner cavity. These redesigned composites can be further applied as fluorescent imaging agent and carriers for preparation of hybrid nanomaterials. CONCLUSIONS: The designing strategy of intrasubunit interfaces opens a new way for future applications of cage-like proteins.


Assuntos
Portadores de Fármacos/química , Ferritinas/química , Ouro/química , Nanopartículas Metálicas/química , Animais , Caenorhabditis elegans/metabolismo , Escherichia coli/genética , Ferritinas/genética , Corantes Fluorescentes/química , Células Hep G2 , Humanos , Mutação , Imagem Óptica
13.
Nat Commun ; 10(1): 778, 2019 02 15.
Artigo em Inglês | MEDLINE | ID: mdl-30770832

RESUMO

Constructing different protein nanostructures with high-order discrete architectures by using one single building block remains a challenge. Here, we present a simple, effective disulfide-mediated approach to prepare a set of protein nanocages with different geometries from single building block. By genetically deleting an inherent intra-subunit disulfide bond, we can render the conversion of an 8-mer bowl-like protein architecture (NF-8) into a 24-mer ferritin-like nanocage in solution, while selective insertion of an inter-subunit disulfide bond into NF-8 triggers its conversion into a 16-mer lenticular nanocage. Deletion of the same intra-subunit disulfide bond and insertion of the inter-subunit disulfide bond results in the conversion of NF-8 into a 48-mer protein nanocage in solution. Thus, in the laboratory, simple mutation of one protein building block can generate three different protein nanocages in a manner that is highly reminiscent of natural pentamer building block originating from viral capsids that self-assemble into protein assemblies with different symmetries.


Assuntos
Dissulfetos/química , Nanoestruturas/química , Sequência de Aminoácidos
14.
J Am Chem Soc ; 140(43): 14078-14081, 2018 10 31.
Artigo em Inglês | MEDLINE | ID: mdl-30336004

RESUMO

Living systems utilize proteins as building blocks to construct a large variety of self-assembled nanoscale architectures. Yet, creating protein-based assemblies with specific geometries in the laboratory remains challenging. Here, we present a new approach that completely eliminates one natural intersubunit interface of multisubunit protein architecture with high symmetry, resulting in reassembly of the protein architecture into one with lower symmetry. We have applied this approach to the conversion of the 24-mer cage-like ferritin into non-native 8-mer protein nanorings in solution. In the crystal structure, such newly formed nanorings connect with each other through hydrogen bonding in a repeating head-to-tail pattern to form nanotubes, and adjacent nanotubes are staggered relative to one another to create three-dimensional porous protein assemblies. The above strategy allows the study of conversion between protein architectures with different geometries by adjusting the interactions at the intersubunit interfaces, and the fabrication of novel bio-nanomaterials with different geometries.

15.
ACS Nano ; 12(11): 11323-11332, 2018 11 27.
Artigo em Inglês | MEDLINE | ID: mdl-30265511

RESUMO

Aromatic-aromatic interactions between natural aromatic amino acids Phe, Tyr, and Trp play crucial roles in protein-protein recognition and protein folding. However, the function of such interactions in the preparation of different dimensional, ordered protein superstructures has not been recognized. Herein, by a combination of the directionality of the symmetry axes of protein building blocks and the strength of the aromatic-aromatic interactions coming from a group of aromatic amino acid residues, we built an engineering strategy to construct protein superlattices. Based on this strategy, substitution of single amino acid residue Glu162 around the C4 rotation axes near the outer surface of 24-mer ferritin nanocage with Phe, Tyr, and Trp, respectively, resulted in 2D and 3D protein superlattices where protein cages are aligned along the C4 axes, imposing a fixed disposition of neighboring ferritins. The self-assembly of these superlattices is reversible, which can be tuned by external stimuli (salt concentration or pH). Moreover, these superlattices can serve as biotemplates for the fabrication of 2D and 3D inorganic nanoparticle arrays.


Assuntos
Aminoácidos Aromáticos/química , Nanopartículas/química , Proteínas/química , Modelos Moleculares , Tamanho da Partícula , Propriedades de Superfície
16.
Protein Sci ; 27(11): 1955-1960, 2018 11.
Artigo em Inglês | MEDLINE | ID: mdl-30099791

RESUMO

Ferritin, a ubiquitous iron storage protein, has a crucial role in innate immunity in arthropods, which have no adaptive immune system. Arthropods are thought to have two types of ferritin molecules: the secreted type and the cytosolic type. Here, we present the first crystal structure of ferritin from crustacean, kuruma prawn (Marsupenaeus japonicus), at 1.16 Å resolution. This shrimp ferritin (MjFer) is the cytosolic type, and its structure shows well-conserved ferritin fold composed of a 4-helix bundle that assembles into a cage-like 24-mer. The structure of MjFer was more similar to those of human and vertebrate ferritins than to that of the secreted-type arthropod ferritin from an insect. MjFer possesses both a ferroxidase site and a nucleation site, which are the main characteristics of vertebrate H and L chain ferritins, respectively. The first crystal structure of crustacean ferritin, MjFer, has exceptionally high quality that provides the detailed structural information of metal moving pathway in ferritin.


Assuntos
Ferritinas/química , Sequência de Aminoácidos , Aminoácidos/química , Animais , Domínio Catalítico , Ceruloplasmina/química , Cristalização/métodos , Humanos , Metais/metabolismo , Modelos Moleculares , Conformação Proteica
17.
Small ; 13(37)2017 10.
Artigo em Inglês | MEDLINE | ID: mdl-28786527

RESUMO

Ferritins are ubiquitous iron storage proteins where Fe(II) sequestration prevents not only its spontaneous oxidation to Fe(III) but also production of toxic free radicals. Recently, scientists have subverted these nature functions and used ferritin cage structures of nanometer dimensions for encapsulation of guest molecules such as anti-cancer drugs or bioactive nutrients based on pH induced ferritin disassembly and reassembly property. However, prior to this study, ferritin nanocage was required to disassemble only under harsh pH conditions (≤2.0 or ≥11.0), followed by reassembly at near neutral pH. Such harsh conditions can cause protein or guest molecules damage to a great extent during this pH-induced unfolding-refolding process. Here, we provide evidence demonstrating that the apoferritin shell is flexible rather than rigid. Indeed, we found that two large complex molecules, uranyl acetate dihydrate and phosphotungstic acid, can reach the cavity of both plant and animal apoferritin followed by mineralization. Moreover, large organic compound such as curcumin and doxorubicin can also be encapsulated within ferritin cavity by its mixing with protein. This strategy will increase the use of ferritin in nanotechnology, and could be also applicable to other shell-like proteins as templates to prepare nanomaterials.


Assuntos
Ferritinas/química , Nanoestruturas/química , Tamanho da Partícula , Apoferritinas/química , Curcumina/química , Ácido Gálico/química , Nanocompostos/química , Nanocompostos/ultraestrutura , Nanoestruturas/ultraestrutura , Espalhamento de Radiação , Espectrometria por Raios X
18.
Crit Rev Food Sci Nutr ; 57(17): 3673-3683, 2017 Nov 22.
Artigo em Inglês | MEDLINE | ID: mdl-26980693

RESUMO

Ferritin is a class of naturally occurring iron storage proteins, which is distributed widely in animal, plant, and bacteria. It usually consists of 24 subunits that form a hollow protein shell with high symmetry. One holoferritin molecule can store up to 4500 iron atom within its inner cavity, and it becomes apoferritin upon removal of iron from the cavity. Recently, scientists have subverted these nature functions and used reversibly self-assembled property of apoferritin cage controlled by pH for the encapsulation and delivery of bioactive nutrients or anticancer drug. In all these cases, the ferritin cages shield their cargo from the influence of external conditions and provide a controlled microenvironment. More importantly, upon encapsulation, ferritin shell greatly improved the water solubility, thermal stability, photostability, and cellular uptake activity of these small bioactive compounds. This review aims to highlight recent advances in applications of ferritin cage as a novel vehicle in the field of food science and nutrition. Future outlooks are highlighted with the aim to suggest a research line to follow for further studies.


Assuntos
Portadores de Fármacos/química , Composição de Medicamentos/métodos , Ferritinas/química , Solubilidade , Animais , Estabilidade de Medicamentos , Ferritinas/metabolismo , Alimentos , Ferro , Estrutura Quaternária de Proteína
19.
ACS Nano ; 10(11): 10382-10388, 2016 11 22.
Artigo em Inglês | MEDLINE | ID: mdl-27934076

RESUMO

Rendering the geometry of protein-based assemblies controllable remains challenging. Protein shell-like nanocages represent particularly interesting targets for designed assembly. Here, we introduce an engineering strategy-key subunit interface redesign (KSIR)-that alters a natural subunit-subunit interface by selective deletion of a small number of "silent" amino acid residues (no participation in interfacial interactions) into one that triggers the generation of a non-native protein cage. We have applied KSIR to construct a non-native 48-mer nanocage from its native 24-mer recombinant human H-chain ferritin (rHuHF). This protein is a heteropolymer composed of equal numbers of two different subunits which are derived from one polypeptide. This strategy has allowed the study of conversion between protein nanocages with different geometries by re-engineering key subunit interfaces and the demonstration of the important role of the above-mentioned specific residues in providing geometric specificity for protein assembly.


Assuntos
Aminoácidos/química , Ferritinas/química , Sequência de Aminoácidos , Humanos , Nanocompostos
20.
Angew Chem Int Ed Engl ; 55(52): 16064-16070, 2016 12 23.
Artigo em Inglês | MEDLINE | ID: mdl-27885765

RESUMO

Protein assemblies with high symmetry are widely distributed in nature. Most efforts so far have focused on repurposing these protein assemblies, a strategy that is ultimately limited by the structures available. To overcome this limitation, methods for fabricating novel self-assembling proteins have received intensive interest. Herein, by reengineering the key subunit interfaces of native 24-mer protein cage with octahedral symmetry through amino acid residues insertion, we fabricated a 16-mer lenticular nanocage whose structure is unique among all known protein cages. This newly non-native protein can be used for encapsulation of bioactive compounds and exhibits high uptake efficiency by cancer cells. More importantly, the above strategy could be applied to other naturally occurring protein assemblies with high symmetry, leading to the generation of new proteins with unexplored functions.

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