Free-Solvent Model of Osmotic Pressure Revisited: Application to Concentrated IgG Solution under Physiological Conditions

Yousef, Mohammed; Datta, Ravindra; Rodgers, V.G.J.

doi:10.1006/jcis.1997.5262

Cited by 33 publications

(80 citation statements)

References 29 publications

(26 reference statements)

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“…Each of these interactions will have unique hydrations, ion binding values, and fractional amounts of protein which need to be considered. Given that the values of hydration and ion binding are available for all proteins in solution, and that the amount of proteins participating in protein-protein interactions is known, the free-solvent model can provide excellent predictions of the crowded protein osmotic pressure [6,7,30].…”

Section: Strong Protein-protein Interactionsmentioning

confidence: 99%

“…The free-solvent model has been described in detail elsewhere for non-interactive protein solutions [6,7]. The following is the development of the generalized free-solvent model which accounts for protein hydration and ion binding as well as protein-protein interactions.…”

Section: Development Of the Free-solvent Model To Include Protein-promentioning

confidence: 99%

“…For a two-chamber osmometer, with the chamber containing the proteins in aqueous solution denoted as compartment II and the chamber containing only the solvent and diffusible ions (proteins are absent) denoted as compartment I, the free-solvent model, with the mole fraction chosen as the appropriate composition variable, describes the osmotic pressure, p, as [6] …”

Section: Development Of the Free-solvent Model To Include Protein-promentioning

confidence: 99%

“…van Laar [4] proposed that solvent-solute interactions are coupled to the observed non-ideal behavior of the osmotic pressure and he argued that the mole fraction is the appropriate concentration variable to describe osmotic pressure. Recently, Yousef et al [6,7] revised the free-solvent model to include protein-ion binding. Further, the revised free-solvent model [6,7] describes the solute as a hydrated macromolecule, which contains a monolayer of water and bound ions, and, upon correcting the mole fraction for these interactions, provides excellent predictions for the observed osmotic pressure of single and binary non-interacting protein solutions.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, Yousef et al [6,7] revised the free-solvent model to include protein-ion binding. Further, the revised free-solvent model [6,7] describes the solute as a hydrated macromolecule, which contains a monolayer of water and bound ions, and, upon correcting the mole fraction for these interactions, provides excellent predictions for the observed osmotic pressure of single and binary non-interacting protein solutions. Once more, the free-solvent model is based on two independently measurable physical parameters, protein hydration and protein-ion binding, [8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Strong Protein-protein Interactionsmentioning

confidence: 99%

Section: Development Of the Free-solvent Model To Include Protein-promentioning

confidence: 99%

Section: Development Of the Free-solvent Model To Include Protein-promentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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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Determining fouling‐independent component of critical flux in protein ultrafiltration using the free‐solvent‐based (FSB) model

Wang

Rodgers

2010

AIChE Journal

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Obtaining protein solvent accessible surface area when structural data is unavailable using osmotic pressure

Bride

Rodgers

2011

AIChE Journal

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Here, we provide an algorithm that predicts solvent accessible surface area (SASA) using concentrated solution osmotic pressure data. Sheep hemoglobin monomer and β‐lactoglobulin are used for verification. Additionally, SASA for structurally unknown calf lens α‐crystallin aggregate is predicted. Using osmotic pressure data, the predicted SASA value for sheep hemoglobin, 22,398 ± 1,244 Å2, was in excellent agreement with computational model predictions (24,304 Å2‐26,100 Å2). Similarly, predicted SASA values for bovine β‐lactoglobulin in pH solutions of pH 5.1, 6.0, and 8.0, were 5,765 ± 1,031 Å2, 6,656 ± 1,082 Å2, and 9,141 ± 1,060 Å2, respectively, were in good agreement with the computationally determined SASA value (7,500 Å2–8,628 Å2). Predicted SASA for the aggregate of calf lens α‐crystallin (800 kDa) was found to be 417,691 ± 16,790 Å2. These results illustrate that this novel method can provide an important experimental alternative in estimating SASA for proteins and, possibly, their complexes in solution. © 2011 American Institute of Chemical Engineers AIChE J, 2012

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Free-Solvent Model of Osmotic Pressure Revisited: Application to Concentrated IgG Solution under Physiological Conditions

Cited by 33 publications

References 29 publications

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

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

Determining fouling‐independent component of critical flux in protein ultrafiltration using the free‐solvent‐based (FSB) model

Obtaining protein solvent accessible surface area when structural data is unavailable using osmotic pressure

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