Thermal aggregation of bovine serum albumin studied by asymmetrical flow field-flow fractionation

Yohannes, Gebrenegus; Wiedmer, Susanne Κ.; Elomaa, Matti; Jussila, Matti; Aseyev, Vladimir; Riekkola, Marja‐Liisa

doi:10.1016/j.aca.2010.07.016

Cited by 112 publications

(86 citation statements)

References 52 publications

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“…The depth beneath the exposed surface over which the XPS measurement is sensitive, which we call the information depth, is 6-10 nm, as determined from the electrons' inelastic mean free path [23] of around 2-3 nm at the energies involved in this work. The information depth is similar in magnitude to the hydrodynamic diameter of native BSA of approximately 7 nm [18]. The similar magnitudes of the XPS information depth and BSA-molecule diameter together with the sudden drop in BSA concentration over one etch layer suggest that the thickness of a single removed etch layer is of similar order to the diameter of the BSA molecule.…”

Section: Resultsmentioning

confidence: 62%

“…A number of researchers have demonstrated that BSA is surface active [1,9,11]. In addition, there is a significant disparity in size between BSA (molecular weight 66,000 g/mol, hydrodynamic radius 3.5 nm [18]) and lactose (molecular weight 342 g/mol, hydrodynamic radius 0.45 nm [19]), which could have an effect on the relative mobility of these molecules in aqueous solution and hence the degree of segregation due to differential diffusion driven by concentration gradients that develop during drying.…”

Section: Introductionmentioning

confidence: 98%

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Coat formation of surface-active proteins on aqueous surfaces during drying

Nijdam

Trouillet

Kachel

et al. 2014

Colloids and Surfaces B: Biointerfaces

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Section: Resultsmentioning

confidence: 62%

Section: Introductionmentioning

confidence: 98%

Coat formation of surface-active proteins on aqueous surfaces during drying

Nijdam

Trouillet

Kachel

et al. 2014

Colloids and Surfaces B: Biointerfaces

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“…Bovine serum albumin (BSA) has been extensively used as a model to study protein aggregation [6,8,24,27,34,35,48,49,51] and fibrillation [10,48]. BSA is essentially an all a protein, which is transformed to b-form upon destabilizing conditions [23,24,36].…”

Section: Introductionmentioning

confidence: 99%

Response Surface Methodology for Optimizing the Bovine Serum Albumin Fibrillation

et al. 2012

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Amyloid fibrils are considered as nanostructures that could be formed by ordered self-assembly of the partially-folded states of many different peptides or proteins. In this study, bovine serum albumin was used as a model protein whose ordered aggregation (fibrillation) was optimized. Response surface methodology (RSM) was used in a design that contained a total of 30 experimental trials. The first 24 were organized in a factorial design and from 25 to 30 involved the replications of the central points. Data obtained from RSM were subjected to the analysis of variance (ANOVA) and analyzed using a second order polynomial equation. Subsequent testing of the suggested experimental parameters was done in vitro with Congo red spectrophotometric assay. Protein concentration, pH, temperature and time of incubation were the variables used in this study. Responses were assessed by measuring absorbance in 540 nm (characteristic of amyloid formation) and maximal wavelength. Concomitant effects of variables were assessed in surface plots that each considered two of the variables. Interestingly, the pattern obtained by monitoring absorbance at 540 nm and absorbance in maximal wavelength were identical in most cases. We are reporting the optimum concentration of protein, pH, temperature and time at 5 mg ml⁻¹, 3.02 and 72 °C and 48 h, respectively. Our findings suggest that use of Congo red spectrophotometric test, as a simple and affordable assay could be suggested as a first test for assessing fibril formation of proteins. Absorbance in maximal wavelength is recommended as a significant indication of fibril formation.

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“…To allow an approximate comparison of molecular weight and hydrodynamic diameter, the example of bovine serum albumin (BSA) can be used. BSA has a molecular weight of 66,000 g mol -1 , which results in a hydrodynamic diameter of approximately 7 nm as determined by asymmetrical flow field-flow fractionation (AF 4 ) (Yohannes et al 2010). That means that a 1000 g mol -1 molecule is around ffiffiffiffiffi 66 3 p times = four times smaller, i.e., around 2 nm.…”

Section: Open Question 2: If Migration Of Enos Occurs What Is the MImentioning

confidence: 99%

Six open questions about the migration of engineered nano-objects from polymer-based food-contact materials: a review

Jokar

Pedersen

Loeschner

2016

Food Additives & Contaminants: Part A

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The use of nanomaterials in food-contact applications has created enormous interest in recent years. The potential migration of engineered nano-objects (ENOs) from food-contact materials (FCMs) is one of the most important concerns regarding potential human exposure to ENOs and health risks. Current research focusing on FCMs has often reached inconsistency regarding migration of ENOs. The scope of this critical review is to give a concise overview of the most relevant aspects of the subject, and to identify and discuss the major open questions in relation to migration of ENOs from FCMs. This includes the very fundamental questions whether ENOs can migrate from FCMs at all and what the potential release mechanisms of ENOs could be. The inconsistency of findings from experimental studies is highlighted based on the example of silver nanoparticle migration from polymer-based FCMs. Challenges in the detection and characterisation of ENOs in migration studies and the suitability of the most frequently used analytical techniques are discussed. Further, this review questions the suitability of standard food simulants and migration test conditions for FCMs as well as of conventional mathematical migration models. Considerations regarding the risk for consumers associated with migrating ENOs from FCMs are discussed. ARTICLE HISTORY

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Thermal aggregation of bovine serum albumin studied by asymmetrical flow field-flow fractionation

Cited by 112 publications

References 52 publications

Coat formation of surface-active proteins on aqueous surfaces during drying

Coat formation of surface-active proteins on aqueous surfaces during drying

Response Surface Methodology for Optimizing the Bovine Serum Albumin Fibrillation

Six open questions about the migration of engineered nano-objects from polymer-based food-contact materials: a review

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