High-performance liquid chromatography as a technique to measure the competitive adsorption of plasma proteins onto latices

Lensen, H.G.W.; Bargeman, D.; Bergveld, Piet; Smolders, C.A.; Feijén, Jan

doi:10.1016/0021-9797(84)90079-1

Cited by 69 publications

(23 citation statements)

References 49 publications

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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%

“…This effect has been observed in both stagnant [83,84] and low shear flow conditions (≈ 500 sec -1 , 225 sec -1 to 2700 sec -1 ) [85,86]. However, with a few exceptions, [87][88][89] there seems to be an overall lack of tools that can study adsorption-desorption of oligomers of same protein other than a few exceptions. Furthermore, it is common to label proteins while studying multi-protein systems or sequential adsorption [92][93][94] despite the fact that labeling may change conformational stability of proteins and also affect adsorption patterns [95][96][97].…”

Section: Introductionmentioning

confidence: 97%

“…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. monomers, dimers, trimers etc.…”

Section: Introductionmentioning

confidence: 99%

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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%

Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

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Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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“…This phenomenon, which is representative of what has been termed the "Vroman effect," has been demonstrated by Vroman and Adams (3) for fibrinogen. In studies involving fibrinogen, IgG, and albumin at long adsorption times, it is observed that the preference for the adsorbent surface decreases in this order (4,5). Nevertheless, when comparing the adsorption affinity of proteins ofdifferent sizes, the differences in their electrical charge and conformational stability and in their hydrophobicity or that of the surface must also be taken into account.…”

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confidence: 99%

Competitive adsorption of human immunoglobulin G and albumin: consequences for structure and reactivity of the adsorbed layer.

Lutanie

Voegel

Schaaf

et al. 1992

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

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The affinity of polyclonal anti-IgG for human IgG adsorbed on silica surfaces was investigated by two complementary techniques, scanning angle reflectometry and 125I radiotracing. Special attention was paid to compare the reactivity of IgG adsorbed directly or by exchange with already adsorbed albumin. In particular it was shown that (i) in the first case (direct adsorption) the reaction between anti-IgG and adsorbed IgG was in the ratio 1:1 and (it) in the second case (adsorption by exchange) there was no reaction.Most natural systems, essentially biofluids, contain different kinds of proteins mutually competing for adsorption at any exposed surface. Understanding the mechanism of competitive protein adsorption is therefore of great interest for the development of biocompatible materials. Extensive work, including adsorption experiments in which single protein solutions and solutions of protein mixtures were used (1, 2), has been carried out to obtain more insight into this phenomenon. Most investigations have been performed with three plasma proteins: (i) fibrinogen, due to its physiological role in hemostasis, (ii) albumin, due to its abundance in plasma, and (iii) IgG, since it is the most important among the globulins.From competitive adsorption experiments it is usually found that the sorbent surface is initially populated by the smaller and more abundantly occurring molecules, which exhibit a faster rate of diffusion. At later stages, these adsorbed molecules must be displaced by other molecules of higher molecular weight having a stronger tendency to adsorb but with a smaller diffusion coefficient. This phenomenon, which is representative of what has been termed the "Vroman effect," has been demonstrated by Vroman and Adams (3) for fibrinogen. In studies involving fibrinogen, IgG, and albumin at long adsorption times, it is observed that the preference for the adsorbent surface decreases in this order (4, 5). Nevertheless, when comparing the adsorption affinity of proteins ofdifferent sizes, the differences in their electrical charge and conformational stability and in their hydrophobicity or that of the surface must also be taken into account. Indeed, Brash and Uniyal (6) have shown that the exchange sequence (albumin, IgG, fibrinogen, fibronectin, factor XII, high molecular weight kininogen) commonly reported on hydrophilic surfaces like glass (7) does not apply to hydrophobic polystyrene or polyethylene.To our knowledge, no results have been reported on the relationship between competitive adsorption and antigenantibody reactions. Competitive adsorption may, however, have implications for the use of antigen-antibody assays involving the adsorption of protein antigens from blood plasma containing other proteins. In this regard, we studied the reactivity of adsorbed IgG toward anti-IgG (IgY) molecules in three situations: IgG molecules were immobilized either alone or from a binary IgG/albumin mixture on a bare silica surface or were adsorbed from an IgG solution onto an albumin-precoated surfa...

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“…41932) was obtained from Serva and characterized as described earlier [13]. Specific surface area 15 m:/g; poly-styrene content 10% (w/w); density 1.0 g/l; diameter latex particles 399 nm according to scanning electron microscopy (SEM).…”

Section: Methodsmentioning

confidence: 99%

Competitive adsorption of plasma proteins at solid—liquid interfaces

Lensen

Breemhaar

Smolders

et al. 1986

Journal of Chromatography B: Biomedical Sciences and Applicatio

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SUMMARYThe competitive adsorption of human serum albumin (HSA), human immuno-7-globulin (HIgG) and human fibrinogen (HFb) onto polystyrene (PS) at 20°C and a pH of 7.35 (phosphate-buffered saline) was studied. Protein adsorption was studied using enzyme immunoassay. The results obtained with the immunoassay were compared with those obtained using radiolabelled proteins. Recent studies revealed that the adsorption behaviour of radiolabelled proteins onto surfaces differs from that of the non-labelled proteins, which may lead to misinterpretation of adsorption data. Differences in the adsorption behaviour of the labelled proteins as compared to non-labelled proteins can possibly be explained by the formation of modified proteins during the labelling procedure as shown by ion-exchange high-performance liquid chromatography (HPLC). The competitive adsorption of HSA, HIgG and HFb onto a PS latex was studied by measuring the depletion of proteins in solution. The decrease in protein concentration in solution was determined by HPLC techniques. A strong preferential adsorption of HFb was observed with maximum adsorption values of 0.6 ug/cm 2.

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High-performance liquid chromatography as a technique to measure the competitive adsorption of plasma proteins onto latices

Cited by 69 publications

References 49 publications

Electrospray–differential mobility analysis of bionanoparticles

Electrospray–differential mobility analysis of bionanoparticles

Competitive adsorption of human immunoglobulin G and albumin: consequences for structure and reactivity of the adsorbed layer.

Competitive adsorption of plasma proteins at solid—liquid interfaces

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