Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
Metallomics ; 7(3): 466-77, 2015 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-25634091

RESUMO

We investigated the uptake of cerium (Ce) dioxide nanoparticles (NPs) by hydroponically grown wheat, pumpkin and sunflower plants. The presence of plant roots in nutrient solution led to a substantial increase in the dissolution of CeO2-NP compared to plant-free medium. Experiments with Zr/CeOx-NP revealed that Ce was not only taken up in the form of NPs, but simultaneously to a significant degree also as dissolved Ce(iii) ions, which then re-precipitated in the form of CeO2-NPs inside the leaves. The contribution of dissolved Ce uptake was particularly large for particles smaller than 10 nm due to their higher dissolution rate. Our data also indicate that the translocation of Ce resulting from NP-root-exposure is species dependent. When Ce was supplied as dissolved ions, sunflower had the highest capacity of Ce-ion accumulation inside the leaves, while there was no significant difference between pumpkin and wheat. We found no Ce translocation from roots into shoots when only NPs bigger than 20 nm were applied. This study highlights that plant root activity can have a significant impact on the dissolution of CeO2-NPs in soil solution and that uptake of dissolved Ce(iii) followed by re-precipitation needs to be considered as an important pathway in studies of CeO2-NP uptake by plants.


Assuntos
Cério/metabolismo , Produtos Agrícolas/metabolismo , Nanopartículas/química , Tamanho da Partícula , Cério/química , Cucurbita/metabolismo , Difusão Dinâmica da Luz , Helianthus/metabolismo , Concentração de Íons de Hidrogênio , Hidroponia , Nanopartículas/ultraestrutura , Folhas de Planta/metabolismo , Raízes de Plantas/metabolismo , Brotos de Planta/metabolismo , Solubilidade , Espectrometria por Raios X , Suspensões , Fatores de Tempo , Triticum/metabolismo , Zircônio/metabolismo
2.
Langmuir ; 29(46): 14117-23, 2013 Nov 19.
Artigo em Inglês | MEDLINE | ID: mdl-24151962

RESUMO

Nanomaterials are increasingly suggested for the selective adsorption and extraction of complex compounds in biomedicine. Binding of the latter requires specific surface modifications of the nanostructures. However, even complicated macromolecules such as proteins can afford affinities toward basic surface characteristics such as hydrophobicity, topology, and electrostatic charge. In this study, we address these more basic physical interactions. In a model system, the interaction of bovine serum albumin and amyloid ß 42 fibrillar aggregates with carbon-coated cobalt nanoparticles, functionalized with various polymers differing in character, was studied. The possibility of rapid magnetic separation upon binding to the surface represents a valuable tool for studying surface interactions and selectivities. We find that the surface interaction of Aß 42 fibrillar aggregates is mostly hydrophobic in nature. Because bovine serum albumin (BSA) is conformationally adaptive, it is known to bind surfaces with widely differing properties (charge, topology, and hydrophobicity). However, the rate of tight binding (no desorption upon washing) can vary largely depending on the extent of necessary conformational changes for a specific surface. We found that BSA can only bind slowly to polyethylenimine-coated nanomagnets. Under competitive conditions (high excess BSA compared to that for ß 42 fibrillar aggregates), this effect is beneficial for targeting the fibrillar species. These findings highlight the possibility of selective extractions from complex media when advantageous basic physical surface properties are chosen.


Assuntos
Peptídeos beta-Amiloides/química , Cobalto/química , Nanoestruturas/química , Fragmentos de Peptídeos/química , Soroalbumina Bovina/química , Animais , Ligação Competitiva , Carbono/química , Bovinos , Polietilenoimina/química , Ligação Proteica , Multimerização Proteica , Estrutura Secundária de Proteína , Propriedades de Superfície
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...