Protein interactions at solid surfaces

Claesson, Per M.; Blomberg, Eva; Fröberg, Johan C.; Nylander, Tommy; Arnebrant, Thomas

doi:10.1016/0001-8686(95)00241-h

Cited by 217 publications

(205 citation statements)

References 133 publications

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“…As shown in a previous study, the Dh of BSM was only twice as large as that of contour length on average. 31 For this reason, while mucins are often depicted as highly coiled polymer chains in literature, 32,33 the mucins in this study are better described as "dumbbell"-like shape in their conformations. 13,14,34 For instance, a recent small angle x-ray scattering study has revealed that highly purified "Orthana" PGM displays double-globular comb structure with two globules of an average radius of 10 nm connected with the intramolecular chain of ca.…”

Section: Pin-on-disk (Pod) Tribometrymentioning

confidence: 90%

Structural and Mechanical Properties of Thin Films of Bovine Submaxillary Mucin versus Porcine Gastric Mucin on a Hydrophobic Surface in Aqueous Solutions

et al. 2016

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The structural and mechanical properties of thin films generated from two types of mucins, namely bovine submaxillary mucin (BSM) and porcine gastric mucin (PGM) in aqueous environment were investigated with several bulk and surface analytical techniques. Both mucins generated hydrated films on hydrophobic polydimethylsiloxane (PDMS) surfaces from 2 spontaneous adsorption arising from their amphiphilic characteristic. But, BSM formed more elastic films than PGM at neutral pH condition. This structural difference was manifested from the initial film formation processes to the responses to shear stresses applied to the films.Acidification of environmental pH led to strengthening the elastic character of BSM films with increased adsorbed mass, whereas an opposite trend was observed for PGM films. We propose that this contrast originates from that negatively charged motifs are present for both the central and terminal regions of BSM molecule, whereas a similar magnitude of negative charges is localized at the termini of PGM molecule. Given that hydrophobic motifs acting as anchor are also localized in the terminal region, electrostatic repulsion between anchoring units of PGM molecules on nonpolar PDMS surface leads to weakening of the mechanical integrity of the films.

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Section: Pin-on-disk (Pod) Tribometrymentioning

confidence: 90%

Structural and Mechanical Properties of Thin Films of Bovine Submaxillary Mucin versus Porcine Gastric Mucin on a Hydrophobic Surface in Aqueous Solutions

et al. 2016

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“…The characterization methods employed can be broadly characterized into solution depletion, optical, spectroscopic, imaging and surface force measurement techniques [81,82]. Most of these techniques operate at stagnant conditions [83,84] or at low shear [85,86] (typically 10 2 sec -1 to 10 3 sec -1 ) and have only rarely [87][88][89] been used for studying competitive adsorption of protein oligomers (i.e.…”

Section: Introductionmentioning

confidence: 99%

Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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The growth of the multibillion dollar bionanoparticle industry has spurred the development of new physical characterization methods. One such method, electrospraydifferential mobility analysis (ES-DMA) constitutes an electrospray for aerosolization of bionanoparticles (such as viruses, gold-nanoparticles, proteins, nanoparticle-protein complexes) and an ion mobility method that operates at atmospheric conditions, and separates bionanoparticles spatially. This dissertation identifies some relevant "problem" areas for ES-DMA by reviewing selected applications.Some such problems are: proteins while passing through ES capillaries are found to interact with it and thus produce time dependent size distributions. Further, it is thought that adsorbed proteins may subsequently desorb and influence size distributions with the ES-DMA which may concomitantly affect quantification of aggregates. These artifacts are studied systematically and it is demonstrated that ES-DMA can quantify adsorption-desorption of complex protein mixtures at high shear rates. Further, it is shown that desorbing proteins do not have a significant effect on size distributions. Another artifact of the ES takes place during the aersolization process. Two units (called monomers) of a bionanoparticle may get encapsulated in the same ES droplet and upon drying of the droplet create artificial dimers thus affecting quantification with ES-DMA. Assuming Poisson distribution, this thesis provides a systematic approach that can be undertaken to eliminate this artifact. A third artifact arises from the low sensitivity of the DMA to size increase. When a ligand (for e.g. protein) adsorbs to a bionanoparticle it creates an increase in the size of the later, which can be used to quantify the amount of ligand adsorbed per bionanoparticle. As ligands can change conformations upon adsorption, using ES-DMA for such applications may be flawed. This issue has been identified and a solution has been provided by integrating a mass analyzer after the ES-DMA.After correcting for these artifacts, this dissertation delves into characterization of different types of bionanoparticles and demonstrates that ES-DMA has several advantages over other traditional techniques such as transmission electron microscopy, size exclusion chromatography, analytical ultracentrifugation, dynamic light scattering and plaque assay and thus has immense potential to become a process analytical technique in biomanufacturing environments. ELECTROSPRAY-DIFFERENTIAL MOBILITY ANALYSIS OF BIONANOPARTICLES

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“…1 Dynamics of protein adsorption have been studied by using electrical, optical, or labeling techniques, which primarily provide information about the amount of adsorbed proteins. The quartz crystal microbalance (QCM), one of the piezoelectric devices, has been traditionally utilized to detect small amounts of materials adsorbed on surface.…”

Section: Introductionmentioning

confidence: 99%

QCM Study of β-Casein Adsorption on the Hydrophobic Surface: Effect of Ionic Strength and Cations

2004

Bulletin of the Korean Chemical Society

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The adsorption kinetics of β-casein on a hydrophobic surface has been studied by means of the quartz crystal microbalance (QCM). The self assembled monolayer of 1-octadecanethiol on a gold coated quartz crystal was used as a hydrophobic surface for adsorption. The adsorption kinetics was monitored in different solution conditions. Formation of monolayer is observed in most cases. At high concentration of protein, micelle formation which is interrupted by high ionic strength of solution is observed. Casein binding cations such as Ca 2+ , Ba 2+ and Al 3+ increase the hydrophobicity of the protein and the multiple layer adsorption occurs. The strong and weak points of the QCM method in the study of protein adsorption are discussed.

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Protein interactions at solid surfaces

Cited by 217 publications

References 133 publications

Structural and Mechanical Properties of Thin Films of Bovine Submaxillary Mucin versus Porcine Gastric Mucin on a Hydrophobic Surface in Aqueous Solutions

Structural and Mechanical Properties of Thin Films of Bovine Submaxillary Mucin versus Porcine Gastric Mucin on a Hydrophobic Surface in Aqueous Solutions

Electrospray–differential mobility analysis of bionanoparticles

QCM Study of β-Casein Adsorption on the Hydrophobic Surface: Effect of Ionic Strength and Cations

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