Effect of high shear rate on stability of proteins: kinetic study

Oliva, Alexis; Santoveña, Ana; Fariña, José B.; Llabrés, Matı́as

doi:10.1016/s0731-7085(03)00223-1

Cited by 53 publications

(36 citation statements)

References 21 publications

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“…65 Multi-angle laser light-scattering measurements showed that in addition to the monomer-dimer transition observed in both albumin samples upon shearing, human serum albumin also formed trimers especially at high shear rates. Since the protein concentration and solvent-air interfaces were considered as fixed factors, the observed differences in the degree of albumin aggregation was attributed to the minor variation in their primary structure.…”

Section: Effects Of Shear Flow On Protein Structure and Functionmentioning

confidence: 99%

“…121,132,133 However, it has been established that the shear-stability of a protein molecule depends on: (i) its primary structure and molecular weight (ii) the magnitude of shear strain and the duration of its application, and (iii) the viscosity of its surrounding medium. 31,64,65 Therefore, these factors must be taken in consideration for a complete understanding of the shear-stability of protein systems. Advancing knowledge in this field will be crucial for the design of processes, especially in the bioprocessing industry, to ensure protein stability, maintain functionality, and promote process yield.…”

Section: Implications In Physiology and Bioprocessingmentioning

confidence: 99%

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The effects of shear flow on protein structure and function

Bekard

Asimakis

Bertolini³

et al. 2011

Biopolymers

172

140

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Toxoplasma gondii usually causes an asymptomatic and then latent infection in human adults; however, a potentially fatal disseminated form can occur in immunocompromised patients. Given that the diagnosis of acute Toxoplasma infection, as opposed to latent disease, relies on finding direct evidence of T. gondii infection in tissue, pathologic examination is critical. There have only been a few reports describing the cytomorphology of Toxoplasma in exfoliative cytology, and no reports of the findings in Thin Prep. In this report, we describe a fatal case of toxoplasmosis in a cardiac transplant patient that was diagnosed by respiratory cytopathology. Although the extracellular organisms were well visualized on the Wright‐Giemsa stained cytospin, they were only faintly seen on the Pap‐stained cytospin trapped within mucin and were not easily appreciated on the ThinPrep slides nor the H&E stained cell block sections. An immunohistochemical stain for Toxoplasma performed on the cell block was strongly positive, and an autopsy performed on the patient confirmed disseminated infection. Our case illustrates that the diagnosis of Toxoplasma in exfoliative cytology specimens can be challenging since organisms are not well visualized on ThinPrep or Pap‐stained material; therefore, Wright‐Giemsa stained material can be particularly helpful. Diagn. Cytopathol. 2012. © 2011 Wiley Periodicals, Inc.

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Section: Effects Of Shear Flow On Protein Structure and Functionmentioning

confidence: 99%

Section: Implications In Physiology and Bioprocessingmentioning

confidence: 99%

The effects of shear flow on protein structure and function

Bekard

Asimakis

Bertolini³

et al. 2011

Biopolymers

172

140

View full text Add to dashboard Cite

show abstract

“…It has been reported for example that shear flows increase protein adsorption [86], which is obviously of interest in the context of the human circulatory system where shear rates can vary from 1 sec -1 to 10 5 sec -1 [90]. However, while protein aggregation has been studied at high shear flow rates (10 6 sec -1 ) [91,92] adsorption to surfaces is yet to be probed under these conditions. Further, it is generally believed that in multi-component systems, smaller proteins adsorb fastest, which are then displaced by larger ones [83,85].…”

Section: Introductionmentioning

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%

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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“…and found that each of these mixtures gave higher anti-albumin Abs than immunization with HSA alone (Lee et al, 2005). This might be an acceptable control were it not for the fact that serum albumin is well known to be an insatiable binder of a plethora of proteins and small molecules (for examples of the vast literature, see: Lin et al, 2004;Coyle et al, 2006;Komatsu et al, 2005;Rozak et al, 2005;Chen et al, 2006) Militello et al, 2004;Oliva et al, 2003). Serum albumin also acts as a molecular chaperone and can be included in the extracellular chaperone family (Marini et al, 2005).…”

Section: P a Hoskisson 1 And G Hobbsmentioning

confidence: 99%