Electrostatic contributions to permeate flux behavior in single bovine serum albumin ultrafiltration

Wang, Yiheng; Rodgers, V.G.J.

doi:10.1016/j.memsci.2010.10.002

Cited by 4 publications

(4 citation statements)

References 30 publications

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“…[46][47][48][49][50][51] However, we have shown that, via our FSB model, the bulk property, osmotic pressure, of self-crowded proteins and crowded binary globular protein solutions can directly provide ion binding and hydration properties of proteins, specifically in the highly crowded regions where the rate of change of osmotic pressure to protein concentration is highly non-linear. [52][53][54][55][56][57][58][59][60][61][62][63] Because the FSB model focuses on protein hydration and ion-binding, it can provide a fortuitous approach in interrogating anion effects on crowded protein solutions.…”

Section: Relevance Of Osmotic Pressure In the Interpretation Of Anionmentioning

confidence: 99%

“…Osmotic pressure does not give direct crystallization information. Nevertheless, a number of researchers have used osmotic pressure to address observed phenomena of proteins in ionic aqueous solutions via protein–protein interactions. − However, we have shown that via our FSB model, the bulk property, osmotic pressure of self-crowded proteins and crowded binary globular protein solutions can directly provide ion binding and hydration properties of proteins, specifically in the highly crowded regions where the rate of change of osmotic pressure to protein concentration is highly nonlinear. − Because the FSB model focuses on protein hydration and ion binding, it can provide a fortuitous approach in interrogating anion effects on crowded protein solutions.…”

Section: Introductionmentioning

confidence: 99%

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Interrogating the Osmotic Pressure of Self-Crowded Bovine Serum Albumin Solutions: Implications of Specific Monovalent Anion Effects Relative to the Hofmeister Series

et al. 2018

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The free-solvent-based (FSB) model and osmotic pressure were used to probe the ion binding and protein hydration for self-crowded bovine serum albumin in 0.15 M NaF, NaCl, NaI, and NaSCN solutions. All experiments were conducted with solutions at pH 7.4. The regressed results of the FSB model behavior to the measured osmotic pressure were excellent, albeit, the osmotic pressure data for NaSCN were noisy. The resulting ion binding and hydration were realistic values and the covariance of the two parameters was exceptionally low, providing substantial credibility to the FSB model. The results showed that the kosmotropic F and neutral Cl solutions generated significantly higher ion binding and protein hydration than the chaotropic solutions of I and SCN. Further, the ionic strength ratio and resulting hydration implied that the chaotropic solutions had substantially higher aggregation than the other salts investigated. Overall, the FSB model provides an additional, complementary tool to contribute to the analysis of crowded protein solutions relative to anions in the Hofmeister series as it can interrogate crowded solutions directly; something that is not possible with many measurement techniques.

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Section: Relevance Of Osmotic Pressure In the Interpretation Of Anionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Interrogating the Osmotic Pressure of Self-Crowded Bovine Serum Albumin Solutions: Implications of Specific Monovalent Anion Effects Relative to the Hofmeister Series

et al. 2018

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“…The free-solvent model has also been shown to provide information about the protein, such as hydration, ion binding, and SASA, when concentrated osmotic pressure data is regressed on [6,7,18,19,[30][31][32][33]. However, with the development of the generalized free-solvent model which considers protein-protein interactions comes some limitations to the ability of the free-solvent model for osmotic pressure data regression.…”

Section: Osmotic Pressure Regressionmentioning

confidence: 99%

A generalized free-solvent model for the osmotic pressure of multi-component solutions containing protein–protein interactions

McBride

Rodgers

2014

Mathematical Biosciences

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a b s t r a c tThe free-solvent model has been shown to have excellent predictability of the osmotic pressure for single and binary non-interactive proteins in aqueous solutions. Here the free-solvent model is extended to be more generalized by including the contributions of intra-and inter-protein interactions to the osmotic pressure of a solution in the form of homo-and hetero-multimers. The solute-solvent interactions are considered to be unique for each homo-and hetero-multimer in solution. The effect of the various generalized free-solvent model parameters on the osmotic pressure are examined for a single protein solution with a homo-dimer, a binary protein solution with no protein-protein interactions, and a binary protein solution with a hetero-dimer. Finally, the limitations associated with the generalized free-solvent model are discussed.

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“…Serious membrane fouling is often caused by substances alone or in mixtures [7][8][9]. In order to improve membrane flux, coagulation is used before a membrane system.…”

Section: Introductionmentioning

confidence: 99%

Effect of aluminum speciation on ultrafiltration membrane fouling by low dose aluminum coagulation with bovine serum albumin (BSA)

Wang

et al. 2015

Journal of Membrane Science

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a b s t r a c tUp to now, many studies have focused on ultrafiltration (UF) membrane fouling when sweep flocculation is the main coagulation mechanism. However, there has been less focus on cases where charge neutralization is the main coagulation mechanism. Herein, UF membrane performance was investigated when bovine serum albumin (BSA) was coagulated with low dose aluminum chloride (AlCl 3 ) or polyaluminum chloride (PACl). For AlCl 3 or PACl, a large flux decline occurred at pH 5.5 and membrane fouling was steadily alleviated with increasing pH, resulting in a strong correlation between membrane flux and the corresponding solution pH. As pH rose, the proportions of Al ms (monomeric and small polymeric alum species) and Al u species (i.e., solid phase Al(OH) 3 ) gradually increased. A correlation was also observed between membrane flux and the proportions of Al ms and Al u . Compared with AlCl 3 , much more serious membrane fouling was induced when BSA was coagulated with PACl, owing to the lower proportions of Al ms and Al u species in the PACl system. For AlCl 3 , the potential fouling mechanism was pore constriction or blocking when the proportions of Al ms and Al u were lower than 62.3 75.1% (pH 6.0), followed by cake layer as the main fouling mechanism. For PACl, however, pore constriction or blocking occurred when the proportions of Al ms and Al u were lower than 35.473.2% (pH 6.5), and cake layer gradually became the main fouling mechanism.

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Electrostatic contributions to permeate flux behavior in single bovine serum albumin ultrafiltration

Cited by 4 publications

References 30 publications

Interrogating the Osmotic Pressure of Self-Crowded Bovine Serum Albumin Solutions: Implications of Specific Monovalent Anion Effects Relative to the Hofmeister Series

Interrogating the Osmotic Pressure of Self-Crowded Bovine Serum Albumin Solutions: Implications of Specific Monovalent Anion Effects Relative to the Hofmeister Series

A generalized free-solvent model for the osmotic pressure of multi-component solutions containing protein–protein interactions

Effect of aluminum speciation on ultrafiltration membrane fouling by low dose aluminum coagulation with bovine serum albumin (BSA)

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