The Effect of Radiolabeling of Human Fibrinogen on Its Adsorption Behaviour on a Polystyrene Surface

Elhorst, J. K.; Olthuis, F.M.F.G.; Bargeman, D.; Smolders, C.A.; Feijén, Jan

doi:10.1177/039139887800100609

Cited by 13 publications

(6 citation statements)

References 19 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%

“…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: 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: 99%

Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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“…Although several investigators claim or assume that the adsorption behavior of labeled proteins does not differ from that of nonlabeled ones, some reports indicate that preferential adsorption of labeled protein may occur (33,34,63).…”

Section: Journal Of Colloid and Interface Science Vol 99 No 1 Maymentioning

confidence: 99%

“…Na 125I was purchased from Amersham (IMS 30). The labeling of proteins was carried out with the chloramine-T method (33). After labeling, 75-85% of the radioactivity was incorporated in the protein, which was determined by thinlayer chromatography (TLC) (64).…”

Section: Hplcmentioning

confidence: 99%

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

Lensen¹,

Bargeman²,

Bergveld³

et al. 1984

Journal of Colloid and Interface Science

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Isotherms of human serum albumin (HSA), human immunoglobulin G (HIgG), and human fibrinogen (HFb) onto a polystyrene (PS)-latex were determined by depletion of protein in the solution, which was either followed by radioactivity measurements or by UV spectroscopy. Different adsorption isotherms for the same protein were obtained when either radioactivity measurements or UV spectroscopy was used as a detection technique. In order to obtain reliable results from competitive protein adsorption experiments, a method based on the use of high-performance liquid chromatography was developed. A strong preferential adsorption of HFb was observed when adsorption studies were carried out with mixtures of HSA, HFb, and HIgG. When adsorption studies were carried out with solutions containing HSA monomer and dimer, a strong preferential adsorption of HSA dimer was also observed.

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“…Nal:SI was purchased from Amersham (IMS 30), U.K. The labelling of proteins was carried out with the chloramine-T method [12]. After labelling, 75--85% of the radioactivity was incorporated into the protein, which was determined by thin-layer chromatography (TLC) [14].…”

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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The Effect of Radiolabeling of Human Fibrinogen on Its Adsorption Behaviour on a Polystyrene Surface

Cited by 13 publications

References 19 publications

Electrospray–differential mobility analysis of bionanoparticles

Electrospray–differential mobility analysis of bionanoparticles

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

Competitive adsorption of plasma proteins at solid—liquid interfaces

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