Liquid−Liquid Equilibrium of Aqueous Two-Phase System Composed of Poly(ethylene glycol) 400 and Sulfate Salts

Martins, João Paulo; Coimbra, Jane Sélia dos Reis; Oliveira, Fabíola Cristina de; Sanaiotti, Guilherme; Silva, César A. S. da; Silva, Luís Henrique Mendes da; Silva, Maria do Carmo H. da

doi:10.1021/je9006162

Cited by 45 publications

(34 citation statements)

References 28 publications

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“…The observed pattern is in agreement with what can be found in literature. Thus, recent studies have also found [18][19][20] found that the phase-forming ability of several ILs and polyethylene glycols increases with increasing alkyl-chain length, probably due to the existence of non-favourable interactions between the saltingout inducing ions and the surfactant non-polar moieties, thus leading to an easier phase disengagement. (4).…”

Section: Resultsmentioning

confidence: 99%

Triton X surfactants to form aqueous biphasic systems: Experiment and correlation

Álvarez

Moscoso

Rodríguez

et al. 2012

The Journal of Chemical Thermodynamics

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Section: Resultsmentioning

confidence: 99%

Triton X surfactants to form aqueous biphasic systems: Experiment and correlation

Álvarez

Moscoso

Rodríguez

et al. 2012

The Journal of Chemical Thermodynamics

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“…The liquid-liquid separation of PEG/salt aqueous solutions is a fundamentally different phenomenon from PEG/protein or salt/protein LLPS, which originate by a combination of hydrophobic and salting-out effects, whose origin has been attributed to the different conformations of the PEG polymer chain in aqueous solution and their respective hydration 24 . Actually, the PEG400/Na 2 SO 4 /H 2 O system is known to generate aqueous two-phase systems 36,56,57 . Figure 2 displays the experimental binodal curve together with liquid-liquid equilibrium tie-lines data for PEG400 + Na 2 SO 4 + H 2 O system at 293.15 K (the temperature used in this work for crystallization experiments and SLS/DLS measurements) 36 .…”

Section: The Role Of Llps In Anti-cd20 Crystallizationmentioning

confidence: 99%

On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS)

Pantuso

Mastropietro

Briuglia

et al. 2020

Sci Rep

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The crystallization of Anti-CD20, a full-length monoclonal antibody, has been studied in the PEG400/ na 2 So 4 /Water system near Liquid-Liquid Phase Separation (LLPS) conditions by both sitting-drop vapour diffusion and batch methods. In order to understand the Anti-CD20 crystallization propensity in the solvent system of different compositions, we investigated some measurable parameters, normally used to assess protein conformational and colloidal stability in solution, with the aim to understand the aggregation mechanism of this complex biomacromolecule. We propose that under crystallization conditions a minor population of specifically aggregated protein molecules are present. While this minor species hardly contributes to the measured average solution behaviour, it induces and promotes crystal formation. The existence of this minor species is the result of the LLPS occurring concomitantly under crystallization conditions. A thorough understanding of protein aggregation behaviour in solution is crucial for the controlled manufacture and formulation of therapeutics and for the development of crystallization-based purification strategies for biological drugs 1-4. Unfortunately, while the state diagram of protein-solvent systems can provide indications about the phase behaviour of biomacromolecules and their stability in solution, the intimate mechanism underlying protein nucleation and crystal growth have not been fully understood yet and, in many cases, it remains elusive. Protein aggregation is directly related to protein-protein interactions and may be strongly related to protein crystallization behaviour 5. Since different types of intermolecular forces are involved in protein interactions, such as electrostatic, van der Waals and hydrophobic 6 , environmental factors like pH, ionic strength and the presence of additives, can drastically alter the intermolecular interaction profile of proteins in solution 7,8. Colloidal and conformational stabilities are the two main factors that govern the existence of a protein aggregate in a solution 9,10. Colloidal stability is a delicate balance between repulsive and attractive forces between proteins, while conformational stability is related to the free energy difference between two molecular states, folded and partially or totally unfolded. Several investigations have found that the melting temperature (T m) and the osmotic second virial coefficient (B 22) can respectively account for the protein conformational 11 and colloidal 12 stability. Both T m and B 22 can be experimentally determined by using correspondingly Dynamic Light Scattering (DLS) and Static Light Scattering (SLS) methods 13. Aggregation induced by thermal unfolding can be monitored by measuring the average hydrodynamic diameter value as a function of temperature, while B 22 describes the first deviation from ideal behaviour of dilute colloidal solutions 14. A positive or negative value of B 22 accounts for a net repulsive or attractive interaction balance, respectively, and could therefore be used t...

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“…15 between the phases in equilibrium, at constant pressure and temperature, and is calculated using the equation 3 [29].…”

Section: Equilibrium Data Of Atpssmentioning

confidence: 99%

Phase diagrams, densities and refractive indexes of poly(ethylene oxide)+organic salts+water aqueous two-phase systems: Effect of temperature, anion and molar mass

Rengifo

Ferreira

et al. 2015

Fluid Phase Equilibria

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Phase diagrams, densities and refractive indexes of poly(ethylene oxide) + organic salts + water aqueous two-phase systems: Effect of temperature, anion and molar mass, Fluid Phase Equilibria http://dx. Graphical abstractHighlights  The segregation process is endothermic and entropically driven for all ATPS.  The biphasic region on the phase diagrams increase as the molar mass of PEO increase.  The biphasic region increased in relation to the anions studied: citrate > tartrate > succinate. AbstractThe application of aqueous two-phase systems (ATPSs) at the industrial level requires systems formed by non-toxic substances to decrease the negative impact on the environment. Organic salts such as sodium citrate, sodium tartrate and sodium succinate have been utilized in order to fulfill this objective. In this work, ATPSs formed by poly(ethylene oxide), PEO, with molar mass 10,000 or 35,000 g mol -1 , organic salts and water, namely PEO10000 + sodium citrate + water, PEO10000 + sodium tartrate + water, PEO10000 + sodium succinate + water and PEO35000 + sodium citrate + water ATPSs at (283.15, 298.15 and 313.15) K have been studied. Effects of temperature, anion and polymer molar mass on the phase diagrams, as well as, the densities and refractive indexes of both phases of the ATPSs were evaluated. The segregation process was endothermic and entropically driven for all ATPSs. The biphasic region on the phase diagrams increased as the molar mass of PEO increased. In addition, the biphasic region also increased in relation to the anions studied: citrate > tartrate > succinate. The consistency of the tie-line data was ascertained by applying the Othmer-Tobias correlation.

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Liquid−Liquid Equilibrium of Aqueous Two-Phase System Composed of Poly(ethylene glycol) 400 and Sulfate Salts

Cited by 45 publications

References 28 publications

Triton X surfactants to form aqueous biphasic systems: Experiment and correlation

Triton X surfactants to form aqueous biphasic systems: Experiment and correlation

On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS)

Phase diagrams, densities and refractive indexes of poly(ethylene oxide)+organic salts+water aqueous two-phase systems: Effect of temperature, anion and molar mass

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