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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.
Biotechnol Adv ; 52: 107835, 2021 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-34520791

RESUMO

Elegant protein assembly to generate new biomaterials undergoes extremely rapid development for wide extension of biotechnology applications, which can be a powerful tool not only for creating nanomaterials but also for advancing understanding of the structure of life. Unique biological properties of proteins bestow these artificial biomaterials diverse functions that can permit them to be applied in encapsulation, bioimaging, biocatalysis, biosensors, photosynthetic apparatus, electron transport, magnetogenetic applications, vaccine development and antibodies design. This review gives a perspective view of the latest advances in the construction of protein-based nanomaterials. We initially start with distinguishable, specific interactions to construct sundry nanomaterials through protein self-assembly and concisely expound the assembly mechanism from the design strategy. And then, the design and construction of 0D, 1D, 2D, 3D protein assembled nanomaterials are especially highlighted. Furthermore, the potential applications have been discussed in detail. Overall, this review will illustrate how to fabricate highly sophisticated nanomaterials oriented toward applications in biotechnology based on the rules of supramolecular chemistry.

3.
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
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.
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.

6.
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
7.
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
8.
Inorg Chem ; 60(10): 7207-7216, 2021 May 17.
Artigo em Inglês | MEDLINE | ID: mdl-33852289

RESUMO

Here, we present a 1.9 Å resolution crystal structure of Mycoplasma Penetrans ferritin, which reveals that its ferroxidase center is located on the inner surface of ferritin but not buried within the four-helix of each subunit. Such a ferroxidase center exhibits a lower iron oxidation activity as compared to the reported ferritin. More importantly, we found that Fe2+ enters into the center via the rarely reported B-channels rather than the normal 3- or 4-fold channels. All these findings may provide the structural bases to explore the new iron oxidation mechanism adopted by this special ferritin, which is beneficial for understanding the relationship between the structure and function of ferritin.


Assuntos
Ceruloplasmina/metabolismo , Ferritinas/metabolismo , Compostos Ferrosos/metabolismo , Mycoplasma/química , Ceruloplasmina/química , Ferritinas/química , Compostos Ferrosos/química , Simulação de Dinâmica Molecular , Mycoplasma/metabolismo , Oxirredução
9.
Food Chem ; 349: 129089, 2021 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-33548881

RESUMO

Protein colloid crystals are considered as high porous soft materials, presenting great potentials in nutrients and drug encapsulation, but protein crystal fabrication usually needs precipitant and high protein concentration. Herein, an easy implemented approach was reported for the construction of protein colloid crystals in diluted solution with shimp ferritin as building blocks by taking advantage of the strength of multiple intermolecular arginine-arginine interactions. The X-ray single-crystal structure reveals that a group of exquisite arginine-arginine interactions between two neighboring ferritin enable them self-assembly into long-range ordered protein soft materials. The arginine-arginine interactions mediate crystal generation favored at pH 9.5 with 200 mM NaCl, and the resulting colloid crystals exhibit high thermal stability (90 °C for 30 min). Importantly, the interglobular cavity in colloid crystals is three times larger in volume than that of intrinsic ferritin cavity in each unit cell, which can be used for molecular encapsulation.


Assuntos
Arginina/química , Artemia/química , Ferritinas/química , Temperatura Alta , Animais , Cápsulas , Porosidade
10.
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
11.
J Colloid Interface Sci ; 582(Pt A): 1-11, 2021 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-32814217

RESUMO

HYPOTHESIS: Hierarchical assembly of naturally occurring assemblies is accurate and responsible for performing various cellular functions. However, Nature's wisdom in navigating the assembly process to desired protein assemblies by the cooperation of multiple noncovalent interactions has been underexploited for protein superstructures constructions. Owing to the chemical diversity of noncovalent interactions, it should be possible to fabricate protein assemblies with novel properties in high efficiency through the cooperation of different noncovalent interaction. EXPERIMENTS: Both charged residues and aromatic residues are introduced on the exterior surface of ferritin centered at their symmetry axes, mixing of complementary variants forms ordered assemblies through the cooperation of two kinds of chemical-diverse noncovalent interactions. The assemblies were further characterized in terms of their assembly behavior, structure, size, assembly kinetics, properties and stabilities. FINDINGS: We utilized both electrostatic and π-π stacking interactions between complementary nanocages to cooperatively trigger the self-assembly into predesigned interleaved hetero-superlattices which exhibit high electrolyte stability and thermal stability. The size of the hetero-superlattices can be well controlled with ranges from nanometers to micrometers in solution in response to external stimuli such as pH and salt concentration. The hetero-superlattice may have the potential applications in hybrid bio-templating, light-harvesting and compartmentalized encapsulation.

12.
ACS Nano ; 2020 Nov 16.
Artigo em Inglês | MEDLINE | ID: mdl-33197176

RESUMO

Protein nanocages represent a class of nanovehicles for a variety of applications. However, precise manipulation of self-assembly behavior of these protein nanocages in response to multiple external stimuli for custom-tailored applications remains challenging. Herein, we established a simple but effective strategy for controlling protein nanocage self-assembly that combines a dual property of His motifs (their significantly pH-dependent protonation state and their capacity to coordinate with transition metals) with its high symmetry. With this strategy, we enabled two different ferritin nanocages to disassemble into protein tetramers under neutral solution by introducing His6 motifs at the 4-fold channel interfaces. Notably, these tetramers are able to self-assemble into ferritin-like protein nanocages in response to multiple external stimuli such as transition metal ions and pH, and vice versa, indicative of a reversible self-assembly process. Furthermore, such His-mediated reversible protein self-assembly has been explored for encapsulation of bioactive cargo molecules within these reconstituted protein nanocages with higher loading efficiency under milder conditions as compared to the reported acid denaturation encapsulation method for ferritin.

13.
Nanomaterials (Basel) ; 10(9)2020 Sep 22.
Artigo em Inglês | MEDLINE | ID: mdl-32971961

RESUMO

Compared with other nanocarriers such as liposomes, mesoporous silica, and cyclodextrin, ferritin as a typical protein nanocage has received considerable attention in the field of food, nutrition, and medicine owing to its inherent cavity size, excellent water solubility, and biocompatibility. Additionally, ferritin nanocage also serves as a versatile bio-template for the synthesis of a variety of nanoparticles. Recently, scientists have explored the ferritin nanocage structure for encapsulation and delivery of guest molecules such as nutrients, bioactive molecules, anticancer drugs, and mineral metal ions by taking advantage of its unique reversible disassembly and reassembly property and biomineralization. In this review, we mainly focus on the preparation and structure of ferritin-based nanocarriers, and regulation of their self-assembly. Moreover, the recent advances of their applications in food nutrient delivery and medical diagnostics are highlighted. Finally, the main challenges and future development in ferritin-directed nanoparticles' synthesis and multifunctional applications are discussed.

14.
Anal Chim Acta ; 1127: 149-155, 2020 Aug 29.
Artigo em Inglês | MEDLINE | ID: mdl-32800118

RESUMO

Methylmercury (MeHg+) as one of the most potent neurotoxins is mainly accumulated in brain, so in vivo imaging detection of MeHg+ in brain is of crucial importance. Herein, we reported a photoluminescent nanosensor for MeHg+ detection in brain by integrating the bioimaging of gold nanoclusters (Au NCs), the fluorescence of Au NCs quenched by MeHg+, and the brain targeting feature of our recently constructed 16-mer shell-like protein (7A). First, Au NCs with 7A as a biotemplate (7A-Au NCs) by a facile and green method in water are fabricated for the first time, the fluorescence of which (∼650 nm) can be quenched by MeHg+ in a dose-dependent manner in vitro. Second, the as-prepared 7A-Au NCs are not only suitable for bioimaging of BBB endothelial cells, but also are an effective probe for bioimaging MeHg+ detection in a brain-specific manner. These findings open a door for MeHg+ detection in the brain of living subjects.


Assuntos
Nanopartículas Metálicas , Compostos de Metilmercúrio , Animais , Encéfalo/diagnóstico por imagem , Células Endoteliais , Ferritinas , Ouro , Camundongos
15.
Carbohydr Polym ; 231: 115689, 2020 Mar 01.
Artigo em Inglês | MEDLINE | ID: mdl-31888818

RESUMO

The antitumor activity of zero-valent selenium (Se0) nanoparticles stabilized by chitosan and its oligosaccharides having molecular weights 3 k, 65 k, and 600 k Da, was investigated. The nanoparticles stabilized with high molecular weight chitosan not only released selenium more easily compared with low molecular weight chitosan, but were also taken up by HepG2 cells more easily through electrostatic effect. Moreover, these were more efficient in inhibiting HepG2 cell viability. High ROS levels of cancer cells could easily induce selenium release from these nanoparticles, and oxidize the less toxic Se0 to highly toxic Se4+. The latter could not only consume antioxidant enzymes, but also cause mitochondrial dysfunction and cell apoptosis. Study of antitumor efficacy and side effect on a HepG2 xenograft BALB/c nude mice model exhibited that CS-Se0NPs had a higher selectivity for cancer cells; however, their effect on normal cells, which have relatively lower ROS levels, was limited.


Assuntos
Proliferação de Células/efeitos dos fármacos , Quitosana/farmacologia , Nanopartículas Metálicas/química , Neoplasias/tratamento farmacológico , Animais , Apoptose/efeitos dos fármacos , Quitosana/química , Células Hep G2 , Xenoenxertos , Humanos , Camundongos , Mitocôndrias/efeitos dos fármacos , Mitocôndrias/patologia , Peso Molecular , Oligossacarídeos/química , Oligossacarídeos/farmacologia , Selênio/química
16.
Chemistry ; 26(14): 3016-3021, 2020 Mar 09.
Artigo em Inglês | MEDLINE | ID: mdl-31820500

RESUMO

Metal-organic frameworks (MOFs) hold great promise for numerous applications. However, proteins, carriers of biological functions in living systems, have not yet been fully explored as building blocks for the construction of MOFs. This work presents a strategy for the fabrication of binary MOFs. Considering octahedral ferritin symmetry, four His2 (His-His) motifs were first incorporated into the exterior surface of a ferritin nanocage near each C4 channel, yielding protein linkers with multiple metal-binding sites (bisH-SF). Secondly, by adding nickel ions to bisH-SF solutions triggers the self-assembly of ferritin nanocages into a porous 3D crystalline MOF with designed protein lattice, where two adjacent ferritin molecules along the C4 symmetry axes are bridged by four dinuclear or tetranuclear nickel clusters depending on Ni2+ concentration. This work provides a simple approach for precise control over a binary protein-metal crystalline framework, and the resulting MOFs exhibited inherent ferroxidase activity and peroxidase-like catalytic activity.


Assuntos
Ferritinas/química , Nanopartículas Metálicas/química , Estruturas Metalorgânicas/química , Níquel/química , Motivos de Aminoácidos , Sítios de Ligação , Catálise , Cristalização , Oxirredução , Peroxidases/metabolismo , Porosidade , Ligação Proteica , Multimerização Proteica
17.
Chem Commun (Camb) ; 55(82): 12344-12347, 2019 Oct 10.
Artigo em Inglês | MEDLINE | ID: mdl-31556881

RESUMO

Human ferritin has been explored as a potential drug nanocarrier, but extreme conditions (pH ≤ 2.0) are required for the encapsulation of drugs. Here, by engineering the AB loop of ferritin, we obtained a new ferritin variant with no new pores, which can disassemble at pH 3.0 or 4.0 and reassemble at pH 7.0. Consequently, under mild conditions, drugs can be encapsulated within this new ferritin nanocage.


Assuntos
Antibióticos Antineoplásicos/farmacologia , Doxorrubicina/farmacologia , Ferritinas/química , Nanopartículas/química , Engenharia de Proteínas , Antibióticos Antineoplásicos/química , Proliferação de Células/efeitos dos fármacos , Doxorrubicina/química , Portadores de Fármacos/química , Humanos , Concentração de Íons de Hidrogênio , Modelos Moleculares , Estrutura Secundária de Proteína
18.
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.

19.
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
20.
Nano Lett ; 19(6): 4023-4028, 2019 06 12.
Artigo em Inglês | MEDLINE | ID: mdl-31099248

RESUMO

Precise manipulation of protein self-assembly by noncovalent interactions into programmed networks to mimic naturally occurring nanoarchitectures in living organisms is a challenge due to its structural heterogeneity, flexibility, and complexity. Herein, by taking advantage of both the hydrophobic forces contributed by the "GLMVG" motif, a kind of amyloidogenic motif (AM), and the high symmetry of protein nanocages, we have built an effective protein self-assembly strategy for the construction of two-dimensional (2D) or three-dimensional (3D) protein nanocage arrays. According to this strategy, "GLMVG" AMs from ß-amyloid 42 were grafted onto the outer surface of a 24-mer ferritin nanocage close to its C4 symmetry channels, initially resulting in the production of subgrade 2D nanocage arrays and ultimately generating 3D highly ordered arrays with a simple cubic packing pattern as the reaction time increases. More importantly, the reversibility and the formation rate of these protein arrays can be modulated by pH. This work provides a de novo design strategy for accurate control over 2D or 3D protein self-assemblies.


Assuntos
Peptídeos beta-Amiloides/química , Ferritinas/química , Nanoestruturas/química , Sequência de Aminoácidos , Concentração de Íons de Hidrogênio , Interações Hidrofóbicas e Hidrofílicas , Modelos Moleculares , Nanoestruturas/ultraestrutura , Análise Serial de Proteínas
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