Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis

Brandes, Natascha; Welzel, Petra B.; Werner, Carsten; Kroh, Lothar W.

doi:10.1016/j.jcis.2006.01.065

Cited by 165 publications

(102 citation statements)

References 58 publications

(98 reference statements)

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“…Widely used methods for probing such effects entail measuring changes in infrared absorbance, circular dichroism, or intrinsic fluorescence after exposure of the interface to protein solution (2,(31)(32)(33)(34)(35)(36). These methods can detect shifts in the average secondary structure of the adsorbed protein layer over time without a priori knowledge of protein structure.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…[15] These structural changes upon adsorption to a surface may result in the loss of biological activity and hence activation of immune response. [16,17] Furthermore, the adsorption of protein molecules on the NP surface changes the surface functionality and hence may strongly influence the translocation behaviour in biological systems. [18,19] However, the mechanistic steps involved in these processes are still far from being understood.…”

Section: Introductionmentioning

confidence: 99%

The Influence of Surface Composition of Nanoparticles on their Interactions with Serum Albumin

et al. 2010

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Interactions between differently functionalised silver and gold nanoparticles (NPs) as well as polystyrene nanoparticles with bovine serum albumin (BSA) are studied using circular dichroism (CD) spectroscopy. It is found that the addition of NPs to the protein solution destroys part of the helical secondary structure of the protein as a result of surface adsorption. From the loss of free protein and hence the extent of their structural change adsorption equilibrium constants are derived. The results reveal that citrate‐coated gold and silver NPs exhibit much stronger interactions with BSA than polymeric or polymer‐coated metallic NPs. It is therefore concluded that for the particles considered, the influence of surface composition on the interaction behaviour dominates that of the core.

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“…In this context, we thought it important and beneficial to clarify the factors affecting the adsorption properties of this protein on a variety of dental materials, to the end of effectively accumulating this protein on these target substrates. Among the works concerning the adsorption of lysozyme on dental materials 10,11) , those in which specific adsorption mechanisms had been clarified or adsorption amount had been quantitatively discussed seem to be relatively few. Among the many methods used to evaluate adsorption, quartz crystal microbalance (QCM) is a powerful one since it can precisely detect even a small amount of adsorbed mass by a simple principle.…”

Section: Introductionmentioning

confidence: 99%

Effect of pH and Addition of Salt on the Adsorption Behavior of Lysozyme on Gold, Silica, and Titania Surfaces Observed by Quartz Crystal Microbalance with Dissipation Monitoring

et al. 2008

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The adsorption behaviors of lysozyme on dentally related Au, SiO2, and TiO2 surfaces were investigated by a quartz crystal microbalance with dissipation monitoring (QCM-D) method. Frequency shifts indicated that while lysozyme (pI 11) was fairly adsorbed on the SiO2 (pI 1.9) surface at both pH 3 and 7, it was adsorbed on TiO2 (pI 6.3) surface only at pH 7. However, adsorption was disturbed by 50 mM NaCl. These results strongly suggested an electrostatic nature of the adsorption behavior. Though a large-scale adsorption of the lysozyme on Au sensor was pH-insensitive, softness of the adlayer as seen from the dissipation profile was pH-dependent, indicating an interaction of another type. With all the surfaces, the small dissipation change indicated a stiff lysozyme adlayer. Results of this study revealed that the controlled electrostatic interaction between the material surface and lysozyme might be a useful method for imparting antibacterial property to the dental materials.

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Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis

Cited by 165 publications

References 58 publications

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

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

The Influence of Surface Composition of Nanoparticles on their Interactions with Serum Albumin

Effect of pH and Addition of Salt on the Adsorption Behavior of Lysozyme on Gold, Silica, and Titania Surfaces Observed by Quartz Crystal Microbalance with Dissipation Monitoring

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