The feasibility of radiolabeling for human serum albumin (HSA) adsorption studies

Scheer, A. Van Der; Feijén, Jan; Elhorst, J. K.; Dagneaux, Paul G.L.C. Krugers; Smolders, C.A.

doi:10.1016/0021-9797(78)90194-7

Cited by 53 publications

(9 citation statements)

References 27 publications

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“…The amounts adsorbed after 24 h of incubation at different HSA or Fg concentrations were compared when using only the labeled solution or a 1:4 mixture of labeled and unlabeled solutions, respectively. The adsorbed radiolabeled amount was five times less with the mixture than with the pure labeled solution, indicating that the adsorption behavior of HSA and Fg on glass and on PS was not affected by radiolabeling, as reported before 51…”

Section: Methodssupporting

confidence: 80%

Dual radiolabeling to study protein adsorption competition in relation with hemocompatibility

Nonckreman

Rouxhet

Dupont‐Gillain

2007

J Biomedical Materials Res

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Human fibrinogen (Fg) and albumin (HSA) were labeled with (3)H and (14)C, respectively. Dual counting allowed the adsorbed amount of the two proteins to be determined simultaneously. Single adsorption, adsorption of the two proteins in competition, but also exchange (substitution by molecules of the same nature) and displacement (desorption under the action of the other protein) experiments were performed on two model surfaces, glass and polystyrene (PS), as well as on pure polyvinylchloride (PVC-s) and on PVC from blood bag (PVC-b). As expected, the adsorbed amount of a single protein is higher on a hydrophobic compared to a hydrophilic surface. When the two proteins are adsorbed in competition, they are found in equal proportion on glass, while HSA is twice more abundant than Fg on PS and PVC-s and about six times more abundant on PVC-b. This trend is related to an increase of the water contact angle of the substrates. For PVC-b, the contact angle is affected by the presence of aliphatic components exposed at the extreme surface, as determined by angle-resolved X-ray photoelectron spectroscopy. In exchange and displacement experiments, the first adsorbed molecules remain dominating on PS while they can be removed from glass. Given the known importance of HSA and Fg adsorption for the fate of materials placed in contact with blood, the method described in this paper may be used as a first approach to orient the design of surfaces with improved hemocompatibility.

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Section: Methodssupporting

confidence: 80%

Dual radiolabeling to study protein adsorption competition in relation with hemocompatibility

Nonckreman

Rouxhet

Dupont‐Gillain

2007

J Biomedical Materials Res

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“…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%

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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“…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%

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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The feasibility of radiolabeling for human serum albumin (HSA) adsorption studies

Cited by 53 publications

References 27 publications

Dual radiolabeling to study protein adsorption competition in relation with hemocompatibility

Dual radiolabeling to study protein adsorption competition in relation with hemocompatibility

Electrospray–differential mobility analysis of bionanoparticles

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

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