Investigating Protein Adsorption via Spectroscopic Ellipsometry

Mora, María F.; Wehmeyer, Jennifer; Synowicki, R. A.; Garcı́a, Carlos D.

doi:10.1007/978-0-387-98161-1_2

Cited by 28 publications

(20 citation statements)

References 163 publications

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“…Aiming to understand the driving forces of such interactions, adsorption processes have been studied with a variety of techniques [5] including reflectometry [6], quartz crystal microbalance [7], atomic force microscopy [8], and fluorescence microscopy [9]. In this regard, spectroscopic ellipsometry (SE) is an attractive alternative for the study of adsorption phenomena because it can provide real-time information regarding the kinetics of the adsorption process as well as the structure of the adsorbed layer for a broad range of adsorbate and substrate materials [10, 11]. Ellipsometry is an optical technique that measures changes in amplitude and phase difference between the parallel ( R P ) and perpendicular ( R S ) components of a polarized light beam upon reflection from a surface [12].…”

Section: Introductionmentioning

confidence: 99%

“…Although there are plenty of examples of the use of Cauchy models in literature [11, 15-17], this approach still suffers from fundamental deficiencies; especially when the adsorption process is to be followed under aqueous environments. Among others, it is relevant to mention that at low coverage a) only small changes in the signal (Ψ and Δ as function of time or λ) are obtained, limiting the sensitivity of the experiment; b) the fitting parameters (A, B and C) could be strongly correlated with the thickness; and c) the system cannot distinguish between similar materials (polymers, proteins, etc) competing for the adsorption sites.…”

Section: Introductionmentioning

confidence: 99%

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Staining proteins: A simple method to increase the sensitivity of ellipsometric measurements in adsorption studies

Nejadnik

Garcı́a

2011

Colloids and Surfaces B: Biointerfaces

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This communication describes a simple way to improve the sensitivity of spectroscopic ellipsometry, when applied to monitor the adsorption of proteins to solid surfaces. The method described herein is based on the reaction of a commercially available dye (Coomassie brilliant blue G) with the adsorbed proteins and the subsequent analysis by spectroscopic ellipsometry. In order to demonstrate the potential advantages of this method, the adsorption of bovine serum albumin to an antifouling coating was also investigated. According to our results, the modification with the dye significantly affects the optical properties of the adsorbed protein layer, which can be represented using a simple optical model (Lorentz). In general, the proposed modification increases the sensitivity of the detection by 2.5 ± 0.4 fold and enables the analysis of thin layers of adsorbed protein not obtainable by conventional methods. These results particularly reveal the importance of the proposed modification for the evaluation of low adsorbing substrates and antifouling coatings.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Staining proteins: A simple method to increase the sensitivity of ellipsometric measurements in adsorption studies

Nejadnik

Garcı́a

2011

Colloids and Surfaces B: Biointerfaces

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“…In addition, NP surfaces may take up proteins depending on their isoelectric points in a rather narrow pH range 68 . It has also been observed that an increase in electrostatic interaction is generally accompanied by a reduction of the modification of the native structure 69 . According to literature reports, hydrophobic interactions tend to dominate the energy balance in most cases tested to date 70 ; however, the effect of electrostatic interactions cannot be ignored 71 .…”

Section:  Effects Of Hydrophobicity/hydrophilicitymentioning

confidence: 98%

Adsorption of Protein on a Au Surface Studied by All-Atom Atomistic Simulations

Wei

Deng

2016

J. Phys. Chem. C

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In this work, the adsorption of protein on Au surface coated by self-assembled monolayers (SAMs) of alkanethiol chains is studied by molecular dynamics simulations with an all-atom model. Particularly, a more realistic embedded-atom method potential has been used to characterize the Au-Au interactions in the system as compared to previous studies. With this all-atom model, many experimental observations have been reproduced from the simulations. It is found that the SAMs have the lowest adsorption energy on Au (111) surface where the alkanethiol chains form a well-ordered (√3x√3) R30° triangular lattice at 300 K. Furthermore, it is confirmed that carboxyl-terminated SAMs are more effective to absorb proteins than the methyl-terminated SAMs. Base on the simulation results, we propose that the experimentally observed aggregation of protein-Au nanoparticle conjugates is mainly due to the electrostatic interactions between protein amino acids and carboxyl-terminated SAMs from multiple Au surfaces. ACKNOWLEDGMENTS

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“…The latter methodology allows calculating not only the adsorbed amount but also the adsorption rate, which could be then used to calculate the probability of attachment for a protein under specific experimental conditions [120-122]. Among other techniques[123-126] that have been applied, adsorption kinetics of proteins can be investigated using quartz crystal microbalance (QCM)[92, 127-130] orellipsometry[131, 132]. QCM has the capability of quantifying extremely small amounts of proteins (mass changes) adsorbedto flat and fixed surfaces by measuring the change in frequency across a quartz crystal.…”

Section: Techniques To Investigate Protein Adsorptionmentioning

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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219

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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Investigating Protein Adsorption via Spectroscopic Ellipsometry

Cited by 28 publications

References 163 publications

Staining proteins: A simple method to increase the sensitivity of ellipsometric measurements in adsorption studies

Staining proteins: A simple method to increase the sensitivity of ellipsometric measurements in adsorption studies

Adsorption of Protein on a Au Surface Studied by All-Atom Atomistic Simulations

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

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