Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 5 de 5
Filtrar
Mais filtros

Base de dados
Ano de publicação
Tipo de documento
Assunto da revista
País de afiliação
Intervalo de ano de publicação
1.
J Am Chem Soc ; 146(11): 7555-7564, 2024 Mar 20.
Artigo em Inglês | MEDLINE | ID: mdl-38456423

RESUMO

Constructing low-dimensional/three-dimensional (LD/3D) perovskite solar cells can improve efficiency and stability. However, the design and selection of LD perovskite capping materials are incredibly scarce for inverted perovskite solar cells (PSCs) because LD perovskite capping layers often favor hole extraction and impede electron extraction. Here, we develop a facile and effective strategy to modify the perovskite surface by passivating the surface defects and modulating surface electrical properties by incorporating morpholine hydriodide (MORI) and thiomorpholine hydriodide (SMORI) on the perovskite surface. Compared with the PI treatment that we previously developed, the one-dimensional (1D) perovskite capping layer derived from PI is transformed into a two-dimensional (2D) perovskite capping layer (with MORI or SMORI), achieving dimension regulation. It is shown that the 2D SMORI perovskite capping layer induces more robust surface passivation and stronger n-N homotype 2D/3D heterojunctions, achieving a p-i-n inverted solar cell with an efficiency of 24.55%, which retains 87.6% of its initial efficiency after 1500 h of operation at the maximum power point (MPP). Furthermore, 5 × 5 cm2 perovskite mini-modules are presented, achieving an active-area efficiency of 22.28%. In addition, the quantum well structure in the 2D perovskite capping layer increases the moisture resistance, suppresses ion migration, and improves PSCs' structural and environmental stability.

2.
Helicobacter ; 29(2): e13066, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-38468575

RESUMO

BACKGROUND: SHP1 has been documented as a tumor suppressor and it was thought to play an antagonistic role in the pathogenesis of Helicobacter pylori infection. In this study, the exact mechanism of this antagonistic action was studied. MATERIALS AND METHODS: AGS, MGC803, and GES-1 cells were infected with H. pylori, intracellular distribution changes of SHP1 were first detected by immunofluorescence. SHP1 overexpression and knockdown were then constructed in these cells to investigate its antagonistic roles in H. pylori infection. Migration and invasion of infected cells were detected by transwell assay, secretion of IL-8 was examined via ELISA, the cells with hummingbird-like alteration were determined by microexamination, and activation of JAK2/STAT3, PI3K/Akt, and ERK pathways were detected by immunoblotting. Mice infection model was established and gastric pathological changes were evaluated. Finally, the SHP1 activator sorafenib was used to analyze the attenuating effect of SHP1 activation on H. pylori pathogenesis in vitro and in vivo. RESULTS: The sub-localization of SHP1 changed after H. pylori infection, specifically that the majority of the cytoplasmic SHP1 was transferred to the cell membrane. SHP1 inhibited H. pylori-induced activation of JAK2/STAT3 pathway, PI3K/Akt pathway, nuclear translocation of NF-κB, and then reduced EMT, migration, invasion, and IL-8 secretion. In addition, SHP1 inhibited the formation of CagA-SHP2 complex by dephosphorylating phosphorylated CagA, reduced ERK phosphorylation and the formation of CagA-dependent hummingbird-like cells. In the mice infection model, gastric pathological changes were observed and increased IL-8 secretion, indicators of cell proliferation and EMT progression were also detected. By activating SHP1 with sorafenib, a significant curative effect against H. pylori infection was obtained in vitro and in vivo. CONCLUSIONS: SHP1 plays an antagonistic role in H. pylori pathogenesis by inhibiting JAK2/STAT3 and PI3K/Akt pathways, NF-κB nuclear translocation, and CagA phosphorylation, thereby reducing cell EMT, migration, invasion, IL-8 secretion, and hummingbird-like changes.


Assuntos
Infecções por Helicobacter , Helicobacter pylori , Animais , Camundongos , Proteínas de Bactérias/metabolismo , Antígenos de Bactérias/metabolismo , Helicobacter pylori/fisiologia , NF-kappa B/metabolismo , Interleucina-8/metabolismo , Proteínas Proto-Oncogênicas c-akt/metabolismo , Fosfatidilinositol 3-Quinases/metabolismo , Infecções por Helicobacter/patologia , Sorafenibe/metabolismo , Células Epiteliais/metabolismo
3.
Angew Chem Int Ed Engl ; 63(32): e202407766, 2024 Aug 05.
Artigo em Inglês | MEDLINE | ID: mdl-38778504

RESUMO

Inverted perovskite solar cells (PSCs) are preferred for tandem applications due to their superior compatibility with diverse bottom solar cells. However, the solution processing and low formation energy of perovskites inevitably lead to numerous defects at both the bulk and interfaces. We report a facile and effective strategy for precisely modulating the perovskite by incorporating AlOx deposited by atomic layer deposition (ALD) on the top interface. We find that Al3+ can not only infiltrate the bulk phase and interact with halide ions to suppress ion migration and phase separation but also regulate the arrangement of energy levels and passivate defects on the perovskite surface and grain boundaries. Additionally, ALD-AlOx exhibits an encapsulation effect through a dense interlayer. Consequently, the ALD-AlOx treatment can significantly improve the power conversion efficiency (PCE) to 21.80 % for 1.66 electron volt (eV) PSCs. A monolithic perovskite-silicon TSCs using AlOx-modified perovskite achieved a PCE of 28.5 % with excellent photothermal stability. More importantly, the resulting 1.55 eV PSC and module achieved a PCE of 25.08 % (0.04 cm2) and 21.01 % (aperture area of 15.5 cm2), respectively. Our study provides an effective way to efficient and stable wide-band gap perovskite for perovskite-silicon TSCs and paves the way for large-area inverted PSCs.

4.
Virulence ; 15(1): 2375549, 2024 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-38982595

RESUMO

CagA is a significant oncogenic factor injected into host cells by Helicobacter pylori, which is divided into two subtypes: East Asian type (CagAE), characterized by the EPIYA-D motif, and western type (CagAW), harboring the EPIYA-C motif. CagAE has been reported to have higher carcinogenicity than CagAW, although the underlying reason is not fully understood. SHIP2 is an intracellular phosphatase that can be recruited by CagA to perturb the homeostasis of intracellular signaling pathways. In this study, we found that SHIP2 contributes to the higher oncogenicity of CagAE. Co-Immunoprecipitation and Pull-down assays showed that CagAE bind more SHIP2 than CagAW. Immunofluorescence staining showed that a higher amount of SHIP2 recruited by CagAE to the plasma membrane catalyzes the conversion of PI(3,4,5)P3 into PI(3,4)P2. This alteration causes higher activation of Akt signaling, which results in enhanced IL-8 secretion, migration, and invasion of the infected cells. SPR analysis showed that this stronger interaction between CagAE and SHIP2 stems from the higher affinity between the EPIYA-D motif of CagAE and the SH2 domain of SHIP2. Structural analysis revealed the crucial role of the Phe residue at the Y + 5 position in EPIYA-D. After mutating Phe of CagAE into Asp (the corresponding residue in the EPIYA-C motif) or Ala, the activation of downstream Akt signaling was reduced and the malignant transformation of infected cells was alleviated. These findings revealed that CagAE hijacks SHIP2 through its EPIYA-D motif to enhance its carcinogenicity, which provides a better understanding of the higher oncogenic risk of H. pylori CagAE.


Assuntos
Motivos de Aminoácidos , Antígenos de Bactérias , Proteínas de Bactérias , Infecções por Helicobacter , Helicobacter pylori , Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases , Humanos , Proteínas de Bactérias/metabolismo , Proteínas de Bactérias/genética , Helicobacter pylori/genética , Helicobacter pylori/patogenicidade , Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/genética , Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo , Antígenos de Bactérias/metabolismo , Antígenos de Bactérias/genética , Infecções por Helicobacter/microbiologia , Transdução de Sinais , Carcinogênese , Ligação Proteica , População do Leste Asiático
5.
Nanomicro Lett ; 16(1): 190, 2024 May 02.
Artigo em Inglês | MEDLINE | ID: mdl-38698298

RESUMO

A considerable efficiency gap exists between large-area perovskite solar modules and small-area perovskite solar cells. The control of forming uniform and large-area film and perovskite crystallization is still the main obstacle restricting the efficiency of PSMs. In this work, we adopted a solid-liquid two-step film formation technique, which involved the evaporation of a lead iodide film and blade coating of an organic ammonium halide solution to prepare perovskite films. This method possesses the advantages of integrating vapor deposition and solution methods, which could apply to substrates with different roughness and avoid using toxic solvents to achieve a more uniform, large-area perovskite film. Furthermore, modification of the NiOx/perovskite buried interface and introduction of Urea additives were utilized to reduce interface recombination and regulate perovskite crystallization. As a result, a large-area perovskite film possessing larger grains, fewer pinholes, and reduced defects could be achieved. The inverted PSM with an active area of 61.56 cm2 (10 × 10 cm2 substrate) achieved a champion power conversion efficiency of 20.56% and significantly improved stability. This method suggests an innovative approach to resolving the uniformity issue associated with large-area film fabrication.

SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA