Adsorption and Relaxation Kinetics of Albumin and Fibrinogen on Hydrophobic Surfaces:  Single-Species and Competitive Behavior

and, Christian F. Wertz; Santore, Maria M.

doi:10.1021/la990089q

Cited by 218 publications

(297 citation statements)

References 60 publications

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“…Protein denaturation on the surface would result in shrinkage of the protein-adsorbed film through the unraveling and flattening of the protein to the surface. Denaturation of surface bound protein can also result in desorption of proteins adjacent to the denaturing protein (27). The specific orientation of BSA on surfaces and the extent of protein denaturation were indeterminate within these experiments, and we shall limit our discussions to more general statements of protein adsorption with regard to adsorbed film thickness.…”

Section: Bsa Adsorption On Sam Coated Siliconmentioning

confidence: 98%

“…The concentration of BSA is similar to the concentration of proteins in cell culture sera (~6 mg/mL), which in turn is near physiological protein concentrations (~40 mg/mL). Protein adhesion studies found in the literature (23,24,26,27,29) have typically used concentrations between 1.0 -0.01 mg/mL, which is the concentration range where the protein-surface adsorption isotherm rise is steepest. By employing concentrations at which the adsorption isotherm has the steepest slope, the effect of surface passivation is more distinct.…”

Section: Bsa Adsorption On Sam Coated Siliconmentioning

confidence: 99%

“…Polyethylene glycol (PEG), or polyethyleneoxide (PEO), functionalized surfaces are examples of hydrophilic coatings that offer excellent resistance to protein and cellular adhesion as both grafted polymer and SAM films (19,20,21,22,23,24). In contrast, hydrophobic surfaces, such as octadecyltrichlorosilane SAMs, tend to adsorb proteins as a monolayer thick biofilm (25,26,27). The current understanding of the difference in protein adhesion is related to the interfacial free energy of the coating in water (surface hydrophobicity), steric repulsion of the functionalized surface against protein (entropy losses in chain conformation and solvent expulsion), and conformational changes allowed by the adsorbing protein (28,29,30).…”

Section: Introductionmentioning

confidence: 99%

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Protein Adhesion on SAM Coated Semiconductor Wafers: Hydrophobic versus Hydrophilic Surfaces

Follstaedt¹,

Cheung²,

Gourley³

et al. 2000

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The interface of biology and semiconductor materials has become an important topic of interest as researchers are merging living organisms with microelectromechanical systems (MEMS) in the pursuit of new microfabricated biomedical devices. Biological cells interface with the semiconductor surface through a host of interactions that are mediated by protein adhesion and film formation. To better understand this interface, we have conducted protein adsorption studies of a model system using bovine serum albumin (BSA) and compared it to the adsorption from a complex protein mixture of cell growth serum on uncoated and self-assembled monolayer (SAM) coated silicon wafers. Several characterization techniques -AFM, ellipsometry, water contact angle, and fluorescence microscopy -were used to evaluate the protein-adsorbed layer. An uncoated silicon surface was most attractive to proteins, forming a 70 Å thick film from a solution of BSA at a concentration comparable to that in cell growth serum. Coating with the hydrophobic octadecyltrimethoxysilane (OTMS) SAM reduced protein adhesion by ~15%. In contrast, a hydrophilic N-(triethoxysilylpropyl)-O-polyethyleneoxide urethane (TESP) SAM inhibited protein adhesion by greater than 50%. Protein adhesion studies with cell growth sera containing complex mixtures of proteins paralleled the BSA adsorption studies, clearly identifying the TESP coated surface as a promising biocompatible coating.4

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Section: Bsa Adsorption On Sam Coated Siliconmentioning

confidence: 98%

Section: Bsa Adsorption On Sam Coated Siliconmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Protein Adhesion on SAM Coated Semiconductor Wafers: Hydrophobic versus Hydrophilic Surfaces

Follstaedt¹,

Cheung²,

Gourley³

et al. 2000

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“…Many researchers also have used a variety of informative techniques [7,8] to perform kinetic measurements of adsorbed protein as a function of time and equilibrium adsorption isotherms. Wertz et al [9] used total internal reflectance fluorescence (TIRF) to infer the orientation and spreading behavior of fibrinogen and lysozyme on hydrophobic and hydrophilic surfaces from kinetic measurements. Schunack et al [10] observed three different conformations of the molecule on the flat surface terraces at low temperature by STM.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of His-tagged peptide to Ni, Cu and Au (100) surfaces: Molecular dynamics simulation

Yang

Zhao

2007

Engineering Analysis with Boundary Elements

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Molecular dynamics (MD) simulations are performed to study the interaction of His-tagged peptide with three different metal surfaces in explicit water. The equilibrium properties are analyzed by using pair correlation functions (PCF) to give an insight into the behavior of the peptide adsorption to metal surfaces in water solvent. The intermolecular interactions between peptide residues and the metal surfaces are evaluated. By pulling the peptide away from the peptide in the presence of solvent water, peeling forces are obtained and reveal the binding strength of peptide adsorption on nickel, copper and gold. From the analysis of the dynamics properties of the peptide interaction with the metal surfaces, it is shown that the affinity of peptide to Ni surface is the strongest, while on Cu and Au the affinity is a little weaker. In MD simulations including metals, the His-tagged region interacts with the substrate to an extent greater than the other regions. The work presented here reveals various interactions between His-tagged peptide and Ni/Cu/Au surfaces. The interesting affinities and dynamical properties of the peptide are also derived. The results give predictions for the structure of His-tagged peptide adsorbing on three different metal surfaces and show the different affinities between them, which assist the understanding of how peptides behave on metal surfaces and of how designers select amino sequences in molecule devices design. r

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“…Such limitations can lead to misinterpretations of apparent interfacial phenomena, which are used to explain the biocompatibility of biomaterials. For example, conventional biophysical methods often find that the average surface protein conformation relaxes from native-like to nonnative-like upon surface adsorption, which is interpreted as evidence for unfolding (11)(12)(13)(14). However, the time scales over which these conformational changes reportedly occur are orders of magnitude longer than typical surface residence times of isolated proteins (15), suggesting that the picture of surfaceinduced spreading may be oversimplified.…”

mentioning

confidence: 99%

Single-molecule resolution of protein structure and interfacial dynamics on biomaterial surfaces

McLoughlin

Kastantin

Schwartz

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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A method was developed to monitor dynamic changes in protein structure and interfacial behavior on surfaces by single-molecule Förster resonance energy transfer. This method entails the incorporation of unnatural amino acids to site-specifically label proteins with single-molecule Förster resonance energy transfer probes for high-throughput dynamic fluorescence tracking microscopy on surfaces. Structural changes in the enzyme organophosphorus hydrolase (OPH) were monitored upon adsorption to fused silica (FS) surfaces in the presence of BSA on a molecule-by-molecule basis. Analysis of >30,000 individual trajectories enabled the observation of heterogeneities in the kinetics of surface-induced OPH unfolding with unprecedented resolution. In particular, two distinct pathways were observed: a majority population (∼ 85%) unfolded with a characteristic time scale of 0.10 s, and the remainder unfolded more slowly with a time scale of 0.7 s. Importantly, even after unfolding, OPH readily desorbed from FS surfaces, challenging the common notion that surface-induced unfolding leads to irreversible protein binding. This suggests that protein fouling of surfaces is a highly dynamic process because of subtle differences in the adsorption/desorption rates of folded and unfolded species. Moreover, such observations imply that surfaces may act as a source of unfolded (i.e., aggregation-prone) protein back into solution. Continuing study of other proteins and surfaces will examine whether these conclusions are general or specific to OPH in contact with FS. Ultimately, this method, which is widely applicable to virtually any protein, provides the framework to develop surfaces and surface modifications with improved biocompatibility.protein adhesion | single-molecule fluorescence | total internal reflection fluorescence microscopy U nderstanding the effect of near-surface environments on protein conformation is critical in many bioengineering and biomedical applications, including biosensing, cell culture, tissue engineering, biocatalysis, and pharmaceutical formulation. Importantly, surface interactions that perturb protein structure can inactivate proteins, as has widely been observed in the case of surface-immobilized enzymes (1-6). Such interactions, by inducing unfolding and subsequent accumulation of freely absorbing proteins on biomaterial surfaces, may trigger unfavorable cellular responses (7-10). However, experimental methods to elucidate both protein structure and interfacial dynamics (e.g., adsorption, diffusion, desorption), particularly in heterogeneous near-surface environments, are virtually nonexistent.Conventional methods to determine surface effects on protein structure are largely ensemble-averaging techniques that provide limited mechanistic insight. Such limitations can lead to misinterpretations of apparent interfacial phenomena, which are used to explain the biocompatibility of biomaterials. For example, conventional biophysical methods often find that the average surface protein conformation relaxes from ...

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Adsorption and Relaxation Kinetics of Albumin and Fibrinogen on Hydrophobic Surfaces: Single-Species and Competitive Behavior

Cited by 218 publications

References 60 publications

Protein Adhesion on SAM Coated Semiconductor Wafers: Hydrophobic versus Hydrophilic Surfaces

Protein Adhesion on SAM Coated Semiconductor Wafers: Hydrophobic versus Hydrophilic Surfaces

Adsorption of His-tagged peptide to Ni, Cu and Au (100) surfaces: Molecular dynamics simulation

Single-molecule resolution of protein structure and interfacial dynamics on biomaterial surfaces

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