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Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: a review.

ABSTRACT: An important consideration for the development of biosensors is the adsorption of the biorecognition element to the surface of a substrate. As the first step in the immobilization process, adsorption affects most immobilization routes and much attention is given into the research of this process to maximize the overall activity of the biosensor. The use of nanomaterials, specifically nanoparticles and nanostructured films, offers advantageous properties that can be fine-tuned to maximize interactions with specific proteins to maximize activity, minimize structural changes, and enhance the catalytic step. In the biosensor field, protein-nanomaterial interactions are an emerging trend that span across many disciplines. This review addresses recent publications about the proteins most frequently used, their most relevant characteristics, and the conditions required to adsorb them to nanomaterials. When relevant and available, subsequent analytical figures of merits are discussed for selected biosensors. The general trend amongst the research papers allows concluding that the use of nanomaterials has already provided significant improvements in the analytical performance of many biosensors and that this research field will continue to grow.

SUBMITTER: Bhakta SA

PROVIDER: S-EPMC4405630 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

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Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: a review.

Bhakta Samir A SA Evans Elizabeth E Benavidez Tomás E TE Garcia Carlos D CD

Analytica chimica acta 20141029

An important consideration for the development of biosensors is the adsorption of the biorecognition element to the surface of a substrate. As the first step in the immobilization process, adsorption affects most immobilization routes and much attention is given into the research of this process to maximize the overall activity of the biosensor. The use of nanomaterials, specifically nanoparticles and nanostructured films, offers advantageous properties that can be fine-tuned to maximize interac ...[more]

PMID: 25892065

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Project description:Asbestos fiber exposure triggers chronic inflammation and cancer. Asbestos fibers can adsorb different types of proteins. The mechanism of this adsorption, not yet completely understood, has been studied in detail mainly with serum albumin and was shown to induce structural changes in the bound protein. The findings of these works regarded mainly the changes of the protein structure, independently of any relation with asbestos-related diseases. For the first time, we have focused our attention to the consequences of the interaction between asbestos fibers and ferritin, a protein involved in iron metabolism, which is strongly modified in asbestos-related diseases. Even if it is known that ferritin can be adsorbed by asbestos fibers, the results of this interaction for the ferritin secondary structure has not previously been studied. One consequence of asbestos-ferritin interaction, is the formation of the so-called ferruginous/asbestos bodies (ABs). In the AB-coating material, the secondary structure of ferritin is modified, and at present, it is unclear whether or not this modification is a direct consequence of the asbestos interaction. In the present study, chrysotile asbestos, more than other asbestos fiber types tested, was found to rapidly bind holo-ferritin, and the presence of iron seemed to play a key role in this process, since iron-free apo-ferritin was adsorbed at a lower level, and iron-saturated chrysotile lost its ferritin-adsorbing capacity. To directly study the details of ferritin adsorption on asbestos fibers, High Resolution Transmission Electron Microscopy (HR-TEM) was employed together with FTIR microspectroscopy and Infrared nanoscopy, which to the best of our knowledge, have not previously been used for this purpose. Chrysotile-bound apo-ferritin underwent a significant change in secondary structure, showing a shift from a prevalent α-helix to a β-sheet conformation. Conversely, the adsorbed holo-ferritin structure appeared to be only weakly modified. These findings add a new potential mechanism to the toxic activities of asbestos: the fibers can modify the structure, and very likely, the function of adsorbed proteins. This, in relation to ferritin, could be a key mechanism in cell iron homeostasis alteration, typically reported in asbestos-related diseases.

Project description:The adsorption of thallium (Tl) onto phyllosilicate minerals plays a critical role in the retention of Tl in soils and sediments and the potential transfer of Tl into plants and groundwater. Especially micaceous minerals are thought to strongly bind monovalent Tl(I), in analogy to their strong binding of Cs. To advance the understanding of Tl(I) adsorption onto phyllosilicate minerals, we studied the adsorption of Tl(I) onto Na- and K-saturated illite and Na-saturated smectite, two muscovites, two vermiculites and a naturally Tl-enriched soil clay mineral fraction. Macroscopic adsorption isotherms were combined with the characterization of the adsorbed Tl by X-ray absorption spectroscopy (XAS). In combination, the results suggest that the adsorption of Tl(I) onto phyllosilicate minerals can be interpreted in terms of three major uptake paths: (i) highest-affinity inner-sphere adsorption of dehydrated Tl+ on a very low number of adsorption sites at the wedge of frayed particle edges of illite and around collapsed zones in vermiculite interlayers through complexation between two siloxane cavities, (ii) intermediate-affinity inner-sphere adsorption of partially dehydrated Tl+ on the planar surfaces of illite and muscovite through complexation onto siloxane cavities, (iii) low-affinity adsorption of hydrated Tl+, especially in the hydrated interlayers of smectite and expanded vermiculite. At the frayed edges of illite particles and in the vermiculite interlayer, Tl uptake can lead to the formation of new wedge sites that enable further adsorption of dehydrated Tl+. On the soil clay fraction, a shift in Tl(I) uptake from frayed edge sites (on illite) to planar sites (on illite and muscovite) was observed with increasing Tl(I) loading. The results from this study show that the adsorption of Tl(I) onto phyllosilicate minerals follows the same trends as reported for Cs and Rb and thus suggests that concepts to describe the retention of (radio)cesium by different types of phyllosilicate minerals in soils, sediments and rocks are also applicable to Tl(I).

Dataset Information

Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: a review.

Publications

Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: a review.

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