The Adsorption–Desorption Cycle. Reversibility of the BSA–Silica System

Giacomelli, Carla E.; Norde, Willem

doi:10.1006/jcis.2000.7219

Cited by 178 publications

(153 citation statements)

References 32 publications

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“…There are two additional peaks on the DTG and DTA curves in the range 200-600°C corresponding with the exothermic breakdown of BSA molecules [44,45]. Due to protein adsorption, its structure is partially denatured and this structure is identical to the thermally denatured form [46,47]. The first peak in the range of 300-321°C on the DTA curve is associated with the removal of weakly bound BSA molecules from the surface of the adsorbent (van der Waals forces) and the second one in the range of 457-527°C-with the decomposition of protein molecules strongly associated with the surface (electrostatic interactions) [48].…”

Section: Resultsmentioning

confidence: 99%

Adsorption and thermal properties of the bovine serum albumin–silicon dioxide system

Wiśniewska

Szewczuk-Karpisz

Sternik

2014

J Therm Anal Calorim

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The adsorption, electrokinetic, thermal and stability properties of the silicon dioxide (silica, SiO 2 )/ bovine serum albumin (BSA) system were determined. All measurements were carried out as a function of solution pH value. The highest amount of BSA absorbed on the silica surface was observed at pH 4.6 [the value close to the BSA isoelectric point (pI)], which is primarily related to the packed albumin conformation and the lack of adsorbentadsorbate electrostatic repulsion. At pH 4.6, largest mass decrease was also noticed (thermogravimetric measurements). At pH 3, 7.6 and 9, the adsorption levels were much lower. This phenomenon is associated with the electrostatic repulsion between the BSA macromolecules and the silica particles as well as the expanded BSA structure. During biopolymer adsorption, the whole solid surface is coated with the albumin macromolecules. Then, the properties of the silica particles become similar to those of the BSA macromolecules. In the presence of albumin, the silica pH iep point is identical to the BSA pI value. It should also be noted that the albumin adsorption affects the SiO 2 suspension stability. The greatest change was observed at pH 3. Under these conditions, the BSA addition causes electrosteric system stabilization.

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Section: Resultsmentioning

confidence: 99%

Adsorption and thermal properties of the bovine serum albumin–silicon dioxide system

Wiśniewska

Szewczuk-Karpisz

Sternik

2014

J Therm Anal Calorim

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“…This is because the conformation of a protein that corresponds to the free energy minimum in solution typically does not correspond to the free energy minimum of this protein once it is in contact with the surface. The surface-protein contact area induces a gain in free energy and hence proteins tend to maximize their footprint through a conformational re-organization as was shown in numerous experimental works [104][105][106][107][108][109][110].…”

Section: Conformational Changesmentioning

confidence: 87%

Understanding protein adsorption phenomena at solid surfaces

Rabe

Verdes

Seeger

2011

Advances in Colloid and Interface Science

1,347

1,239

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Protein adsorption at solid surfaces plays a key role in many natural processes and has therefore promoted a widespread interest in many research areas. Despite considerable progress in this field there are still widely differing and even contradictive opinions on how to explain the frequently observed phenomena such as structural rearrangements, cooperative adsorption, overshooting adsorption kinetics, or protein aggregation. In this review recent achievements and new perspectives on protein adsorption processes are comprehensively discussed. The main focus is put on commonly postulated mechanistic aspects and their translation into mathematical concepts and model descriptions. Relevant experimental and computational strategies to practically approach the field of protein adsorption mechanisms and their impact on current successes are outlined.

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“…Such a multilayered adsorption scheme can be explained as follows [157]: first a layer of protein adsorbs to the surface and denatures, this promotes the exposure of hydrophobic residues of the first layer of protein which then [158][159][160][161][162]. After ≈ 30 capillary volumes of flushing, the amount of BSA remaining on the surface is estimated to be ≈ 2.8 mg/m 2 , which is close to the theoretical coverage of 3.2 mg/m 2 for a monolayer.…”

Section: Methodsmentioning

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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The Adsorption–Desorption Cycle. Reversibility of the BSA–Silica System

Cited by 178 publications

References 32 publications

Adsorption and thermal properties of the bovine serum albumin–silicon dioxide system

Adsorption and thermal properties of the bovine serum albumin–silicon dioxide system

Understanding protein adsorption phenomena at solid surfaces

Electrospray–differential mobility analysis of bionanoparticles

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