Interfacial rheology of blood proteins adsorbed to the aqueous-buffer/air interface

Ariola, Florly S.; Krishnan, Anandi; Vogler, Erwin A.

doi:10.1016/j.biomaterials.2006.02.005

Cited by 52 publications

(61 citation statements)

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“…However, labeling may change the conformation stability of proteins, and affect their adsorption behavior or even promote aggregation in proteins [87,95,96]. To avoid the adverse effects of labeling, other "label-free" tools have been employed such as size exclusion chromatography [87,95,96], electrophoresis [128], ellipsometry [132,133], spectroscopy [134], surface plasmon resonance [101], quartz crystal microbalance [135], tensiometry [132], reflectrometry [136], shear rheology [125], surface force apparatus [137] and imaging techniques [138]. However, there are only a few reports where these tools have been employed on oligomers (monomers, dimers etc) of the same protein [87][88][89].…”

Section: Oligomeric Protein Adsorption-desorption To Es Silica Capillmentioning

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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Section: Oligomeric Protein Adsorption-desorption To Es Silica Capillmentioning

confidence: 99%

Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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“…Our recent work has focused on energy-and-mass-balance in protein adsorption from stagnant solutions [5][6][7][8]10,[21][22][23][24][25][26], motivated by the idea that these complimentary measures of adsorption for a broad range of proteins should clarify unresolved mechanistic issues such as adsorption reversibility, formation of adsorbed multilayers, and applicability of thermodynamic models. This work has emphasized that adsorption is a partitioning process [27,28] distributing both protein and water molecules between the bulk-solution phase and a three-dimensional (3D) interphase region (Guggenheim surface construction [28,29]).…”

Section: Published In Final Edited Form Asmentioning

confidence: 99%

“…The Random Sequential Adsorption (RSA) model [14][15][16], and the venerable Langmuir adsorption isotherm [17][18][19][20] from which RSA models ultimately originate, are implicitly energy-barrier models as well. Here, net adsorption is controlled by opposing adsorption/desorption rates which, according to activated-rate theory, are moderated by activation energy barriers, with lower barriers corresponding to faster rates.Our recent work has focused on energy-and-mass-balance in protein adsorption from stagnant solutions [5][6][7][8]10,[21][22][23][24][25][26], motivated by the idea that these complimentary measures of adsorption for a broad range of proteins should clarify unresolved mechanistic issues such as adsorption reversibility, formation of adsorbed multilayers, and applicability of thermodynamic models. This work has emphasized that adsorption is a partitioning process [27,28] distributing both protein and water molecules between the bulk-solution phase and a three-dimensional (3D) interphase region (Guggenheim surface construction [28,29]).…”

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confidence: 99%

“…In other words, the interface (interphase) should properly regarded as a volume comprised of both 2D surface and subsurface region -not just 2D surface alone. This distinction between 2D and 3D becomes particularly important in the event of multilayer adsorption, as has been shown to occur for proteins by a number of investigators using a variety of experimental methods over the last twenty years or so [5,6,10,22,24,26,[55][56][57][58][59][60][61][62][63][64].A primary issue with the 2D model applied to the interpretation of principal observations (i) and (ii) of the preceding section is that it eliminates an important degree-of-freedom that allows adsorbate concentration to vary independent of adsorbed mass. Partly because of this, we suspect, modern embellishments of RSA theory are forced to embrace an ever-increasing number of variables to explain all experimental outcomes (see, as a recent example, ref.…”

mentioning

confidence: 99%

“…This interphase dehydration step is slow relative to diffusion of protein into the interphase (step 2) because it requires organization, interaction, and concentration of protein molecules into a loose interfacial network like that inferred from various studies including neutron reflectometry [67,68] , interfacial rheology [26], and interfacial tensiometry [6] (see also citations in ref.…”

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confidence: 99%

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Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Barnthip¹,

Noh²,

Leibner³

et al. 2008

Biomaterials

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Time-dependent energetics of blood-protein adsorption are interpreted in terms of a slowlyconcentrating three-dimensional interphase volume initially formed by rapid diffusion of protein molecules into an interfacial region spontaneously formed by bringing a protein solution into contact with a physical surface. This modification of standard adsorption theory is motivated by the experimental observation that interfacial tensions of protein-containing solutions decrease slowly over the first hour to a steady-state value while, over this same period, the total adsorbed-protein mass is constant (for lysozyme, 15 kDa; albumin, 66 kDa; prothrombin, 72 kDa; IgG, 160 kDa; fibrinogen, 341 kDa studied in this work). These seemingly divergent observations are rationalized by the fact that interfacial energetics (tensions) are explicit functions of solute chemical potential (concentration), not adsorbed mass. Hence, rates-of-interfacial-tension-change parallel a slow interphase concentration effect whereas solution depletion detects a constant interphase composition within the time frame of experiment. A straightforward mathematical model approximating the perceived physical situation leads to an analytic formulation that is used to compute time-varying interphase volume and protein concentration from experimentally-measured interfacial tensions. Derivation from the fundamental thermodynamic adsorption equation verifies that protein adsorption from dilute solution is controlled by a partition coefficient at equilibrium, as is observed experimentally at steady state. Implications of the alternative interpretation of adsorption kinetics on biomaterials and biocompatibility are discussed. KeywordsProtein adsorption; kinetics; interfacial energetics; interphase; surface; radiometry IntroductionProtein-adsorption kinetics are of practical importance in biomaterials because adsorption rates have been implicated as a cause of selective protein adsorption. For example, the so-called Vroman Effect is commonly thought to occur because low-molecular-weight proteins *Author to whom correspondence should be addressed EAV3@PSU.EDU. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Author ManuscriptBiomaterials. Author manuscript; available in PMC 2009 July 1. Published in final edited form as:Biomaterials. presumably arriving first at a surface immersed in a multi-component solution are displaced by higher-molecular-weight proteins arriving later (see refs. and citations therein). The final adsorbed-protein composition is thus purported to be achieved through a complex se...

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Control of the blood–polymer interface by plasma treatment

Dumitrascu

Borcia

2008

J Biomed Mater Res

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Plasma that is generated using dielectric barrier discharge is used to modify the surface properties of polymers used in medicine, at atmospheric pressure. Treatments are performed on films of polyamide-6, high density polyethylene, polymethylmetacrylate, and polytetrafluorethylene, selected for their medical applications. The plasma treatment conditions are discussed, in relation with relevant parameters for the adhesion properties, like the surface energy components, interfacial tension, surface topography, structural changes, and chemical composition. The interface properties are analyzed using the most important fluids implicated in the interfacial events related to the coagulation process at the interface of blood-polymer surface, respectively, water, whole blood, fibrinogen, and albumin. The physical and chemical modification of the surface is theoretically favorable to the interaction of the polymer with the blood and its components, by means of interfacial tension reduction, polarity increase, cleaning, ordering of molecular chains, functionalization, and stabilization effects.

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Interfacial rheology of blood proteins adsorbed to the aqueous-buffer/air interface

Cited by 52 publications

References 53 publications

Electrospray–differential mobility analysis of bionanoparticles

Electrospray–differential mobility analysis of bionanoparticles

Volumetric interpretation of protein adsorption: Kinetic consequences of a slowly-concentrating interphase

Control of the blood–polymer interface by plasma treatment

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