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










Base de dados
Intervalo de ano de publicação
1.
Heliyon ; 9(3): e14693, 2023 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-37101480

RESUMO

In this study, the anticorrosion potential of carboxylic compounds; Lanthanum 4-hydroxycinnamate La(4OHCin)3, Cerium 4-hydroxycinnamate Ce(4OHCin)3 and Praseodymium 4-hydroxycinnamate Pr(4OHCin)3 for the protection of Al-Cu-Li alloy was investigated in 3.5% NaCl solution using electrochemical tests (EIS and PDP), scanning electron microscopy (SEM) and X-ray photoelectron spectroscopy (XPS). The findings achieved show a very good correlation between electrochemical responses and surface morphologies of the exposed alloy, indicating a modification of the surface by precipitation of the inhibitor species, leading to effective protection against corrosion. At optimum concentration 200 ppm, the trend of inhibition efficiency η (%) increases in the order Ce(4OHCin)3 93.35% > Pr(4OHCin)3 85.34% > La(4OHCin)3 82.25%. XPS complemented the findings by detecting and providing information about the oxidation states of the protective species.

2.
J Microsc ; 288(1): 10-15, 2022 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-35916115

RESUMO

Convergent beam electron diffraction (CBED) was used to profile the thickness of aluminium alloys foils prepared by using the twinjet electropolishing method. The two-beam CBED condition was obtained by exciting the { 200 } $\{ {200} \}$ and { 111 } $\{ {111} \}$ aluminium diffracted g-vector. The aluminium alloy foil thicknesses were calculated at different distances from the sample hole edge. In areas where only one Kossel-Möllenstedt (K-M) minima fringe was obtained, the thickness was determined by matching the experimental with simulated convergent beam diffraction patterns. In areas far away from the sample edge, the thickness of foils was high enough to generate at least two (K-M) minima fringes, required for linear regression fitting.

3.
Chem Res Toxicol ; 35(3): 529-537, 2022 03 21.
Artigo em Inglês | MEDLINE | ID: mdl-35175047

RESUMO

Considering the protective ability of proteins and the potential toxicity of free Cu(II), it was proposed herein that the co-presence of protein could play an important role in suppressing the toxicity of free Cu(II) to the stability of bioactive quercetin if a flavonoid-protein-Cu(II) complex could be formed. In this study, the interaction between quercetin (a major flavonoid in the human diet) and bovine serum albumin (BSA) was investigated in the absence and presence of free Cu(II). The results demonstrated that both quercetin and free Cu(II) had a strong ability to quench the intrinsic fluorescence of BSA through a static procedure (i.e., formation of a BSA-monoligand complex). Site marker competitive experiments illustrated that the binding of both quercetin and Cu(II) to BSA mainly took place in subdomain IIA. The quenching process of free Cu(II) with BSA was easily affected by quercetin, and the increased binding capacity possibly resulted from the generation of a ternary quercetin-BSA-Cu(II) complex. The stability and free radical scavenging activity of bioactive quercetin during incubation was promoted in the BSA-diligand complex relative to a quercetin-Cu(II) complex. A quercetin-Cu(II) system could generate reactive oxygen species such as hydrogen peroxide (H2O2) and hydroxyl radicals (•OH), which were significantly inhibited upon BSA binding. Consistently, the cytotoxicity of the quercetin-Cu(II) system to endothelial cells was decreased in the BSA-diligand complex, where the co-presence of BSA played an important role. These results suggest the possibility and advantage of developing albumin-based carriers for the protection of bioactive components and suppression of Cu(II) toxicity in their biomedical and nutritional applications.


Assuntos
Cobre/toxicidade , Quercetina , Soroalbumina Bovina , Células Endoteliais/metabolismo , Flavonoides/química , Humanos , Peróxido de Hidrogênio/farmacologia , Ligação Proteica , Quercetina/química , Quercetina/farmacologia , Soroalbumina Bovina/química , Espectrometria de Fluorescência
4.
Chem Res Toxicol ; 34(6): 1672-1680, 2021 06 21.
Artigo em Inglês | MEDLINE | ID: mdl-33861588

RESUMO

We previously demonstrated that apolipoprotein A-I (apoA-I), the major protein component of high-density lipoprotein (HDL), is an important target for myeloperoxidase (MPO)-catalyzed tyrosine chlorination in the circulation of subjects with cardiovascular diseases. Oxidation of apoA-I by MPO has been reported to deprive HDL of its protective properties. However, the potential effects of MPO-mediated site-specific tyrosine chlorination of apoA-I on dysfunctional HDL formation and atherosclerosis was unclear. Herein, Tyr192 in apoA-I was found to be the major chlorination site in both lesion and plasma HDL from humans with atherosclerosis, while MPO binding to apoA-I was demonstrated by immunoprecipitation studies in vivo. In vitro, MPO-mediated damage of lipid-free apoA-I impaired its ability to promote cellular cholesterol efflux by the ABCA1 pathway, whereas oxidation to lipid-associated apoA-I inhibited lecithin:cholesterol acyltransferase activation, two key steps in reverse cholesterol transport. Compared with native apoA-I, apoA-I containing a Tyr192 → Phe mutation was moderately resistant to oxidative inactivation by MPO. In high-fat-diet-fed apolipoprotein E-deficient mice, compared with native apoA-I, subcutaneous injection with oxidized apoA-I (MPO treated) failed to mediate the lipid content in aortic plaques while mutant apoA-I (Tyr192 → Phe) showed a slightly stronger ability to reduce the lipid content in vivo. Our observations suggest that oxidative damage of apoA-I and HDL involves MPO-dependent site-specific tyrosine chlorination, raising the feasibility of producing MPO-resistant forms of apoA-I that have stronger antiatherosclerotic activity in vivo.


Assuntos
Apolipoproteína A-I/metabolismo , Lipoproteínas HDL/metabolismo , Peroxidase/metabolismo , Adulto , Animais , Apolipoproteína A-I/administração & dosagem , Apolipoproteína A-I/sangue , Aterosclerose , Halogenação , Humanos , Injeções Subcutâneas , Camundongos , Camundongos Knockout para ApoE , Peroxidase/sangue , Tirosina/metabolismo
5.
Annu Int Conf IEEE Eng Med Biol Soc ; 2019: 6561-6564, 2019 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-31947345

RESUMO

Accurate segmentation of pediatric echocardiography is an essential preprocessing step for a wide range of analysis tasks. Currently, it highly relies on sonographer's manual segmentation, which is time-consuming and redundant, and therefore might lead to mistakes. In this paper, we present a deep learning method based on Bilateral Segmentation Network (BiSeNet) to fully automatic segment pediatric echocardiography images in 4 chamber view. BiSeNet consists of two paths, a spatial path for capturing low-level spatial features, and a context path for exploiting high-level context semantic features. In addition, a feature fusion module is used to fuse features learned by both the two paths. Experiments based on our selfcollected dataset shows that our method achieves 0.932, and 0.908 in term of Dice index in the left ventricle and left atrium segmentation task, which outperforms different state-of-the-art U-Net architectures.


Assuntos
Ecocardiografia , Processamento de Imagem Assistida por Computador , Automação , Criança , Aprendizado Profundo , Ventrículos do Coração , Humanos
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...