Adsorption of proteins to thin-films of PDMS and its effect on the adhesion of human endothelial cells

Chumbimuni‐Torres, Karin Y.; Coronado, Ramon E.; Mfuh, Adelphe; Castro-Guerrero, Carlos Fernando; Silva, María Fernanda; Negrete, George R.; Bizios, Rena; Garcı́a, Carlos D.

doi:10.1039/c1ra00198a

Cited by 86 publications

(80 citation statements)

References 89 publications

(123 reference statements)

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“…A relatively high concentration of enzyme (i.e., 1 µg/mL) was chosen for immobilization to maintain their native conformation (maximum enzymatic activity). [21][22][23] The freshly prepared enzyme-loaded microchip was used for AA oxidation. Fig.…”

Section: On-chip Ascorbic Acid Oxidationmentioning

confidence: 99%

Interference-blind microfluidic sensor for ascorbic acid determination by UV/vis spectroscopy

Fernandes

Cardoso

et al. 2016

Sensors and Actuators B: Chemical

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A microfluidic sensor is developed and targeted at specific ingredients determination in drug/food/beverage matrices. The surface of a serpentine polydimethylsiloxane (PDMS) microchannel is modified by enzyme via physisorption. When solutions containing target ingredients pass through the microfluidic channel, enzyme-catalyzed reaction occurs and only converts the target molecules to its products. The whole process is monitored by an end-channel UV/vis spectroscopic detection. Ascorbate oxidase and L-ascorbic acid (AA) are taken as enzyme-substrate model in this study to investigate the feasibility of using the developed strategy for direct quantification of AA in standard solutions and complex matrices. A dietary supplement product, vitamin C tablet, is chosen as a model matrix to test the microfluidic bio-sensor in real-sample analysis. The results illustrate that the established microfluidic biosensor exhibits good reproducibility, stability, and anti-interference property. Technically, it is easy to realize, depends on low investment in chip fabrication, and simple instrumental procedure, where only UV/vis spectrophotometer is required. To sum up, the developed strategy is economical, specific, and accurate, and can be potentially used for fast quantification of ingredient in samples with complex matrix background. It is promising to be widely spread in food industry and quality control department.

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Section: On-chip Ascorbic Acid Oxidationmentioning

confidence: 99%

Interference-blind microfluidic sensor for ascorbic acid determination by UV/vis spectroscopy

Fernandes

Cardoso

et al. 2016

Sensors and Actuators B: Chemical

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“…However, when multiple experiments were analyzed, significant increases in the MSE value were obtained, indicating that the proposed model was not able to accurately describe the optical properties of the sample and therefore may not represent the physical meaning of the measurement. Therefore, and in order to consider the possibility of GOx penetrating into the structure of the polymer, the EMA layer was modified to include the protein (also described with a Cauchy function, n (λ) = 1.45 + 0.01·λ −2 ) [33, 40, 41] as an additional component. The resulting model, schematically shown in Figure 4B, allowed calculating changes in the total thickness of the substrates as well as the relative contribution of the protein to the film.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of glucose oxidase to nanostructured films of polystyrene-block-poly(2-vinylpyridine)

Bhakta¹,

Benavidez²,

Garcı́a³

2014

Journal of Colloid and Interface Science

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A critical step for the development of biosensors is the immobilization of the biorecognition element to the surface of a substrate. Among other materials that can be used as substrates, block copolymers have the untapped potential to provide significant advantages for the immobilization of proteins. To explore such possibility, this manuscript describes the fabrication and characterization of thin-films of polystyrene-block-poly(2-vinylpyridine) (PS-b-P2VP). These films were then used to investigate the immobilization of glucose oxidase, a model enzyme for the development of biosensors. According to the results presented, the nanoporous films can provide significant increases in surface area of the substrate and the immobilization of larger amounts of active enzyme. The characterization of the substrate-enzyme interface discussed in the manuscript aims to provide critical information about relationship between the surface (material, geometry, and density of pores), the protein structure, and the immobilization conditions (pH, ionic strength, and protein concentration) required to improve the catalytic activity and stability of the enzymes. A maximum normalized activity of 3300 ± 700 U m−2 was achieved for the nanoporous film of PS-b-P2VP.

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“…Since it measures the ratio of two values originated by the same signal, the measurements are highly accurate and reproducible. The measurements are complementary to the information obtained by QCM and can be used to determine the optical properties of asubstrate and the thickness of multiple layers on the surface.The technique is simple, nondestructive, has angstrom resolution, and has the capability of allowing the observation of the adsorption process inreal time[94, 134, 135]. The use of imaging ellipsometry can also provide spatial resolution of protein binding [136].…”

Section: Techniques To Investigate Protein Adsorptionmentioning

confidence: 99%

“…Albumin (and most commonly BSA) is a heart-shaped soft protein with a molecular weight of 66.5 kDa and an IEP of 4.8 [108]. Because BSA typically exhibits significant surface-induced spreading upon adsorption, a stable layer of the protein can be formed under a wide number of conditions in less than 1 h [135, 205, 303]. For these reasons (and its low cost), it has been extensively used as a model protein to study adsorption [68, 80, 110, 134, 137, 139, 304, 305], to aid in the suspension of CNT [306], and to block the remaining sites of surfaces after the immobilization of a biorecognition element [250, 260, 294, 307].…”

Section: Adsorbedproteinsmentioning

confidence: 99%

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

Bhakta

Evans

Benavidez

et al. 2015

Analytica Chimica Acta

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222

116

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An important consideration for the development of biosensors is the adsorption of the bio recognition 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 bio sensor. The use of nanomaterials, specifically nanoparticles and nanostructured films, offers advantageous properties that can be fine-tuned for interaction 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.

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Adsorption of proteins to thin-films of PDMS and its effect on the adhesion of human endothelial cells

Cited by 86 publications

References 89 publications

Interference-blind microfluidic sensor for ascorbic acid determination by UV/vis spectroscopy

Interference-blind microfluidic sensor for ascorbic acid determination by UV/vis spectroscopy

Immobilization of glucose oxidase to nanostructured films of polystyrene-block-poly(2-vinylpyridine)

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

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