Protein‐protein and protein‐salt interactions in aqueous protein solutions containing concentrated electrolytes

Curtis, Robin; Montaser, Akbar; Prausnitz, John M.; Blanch, Harvey W.

doi:10.1002/(sici)1097-0290(19980520)58:4<451::aid-bit13>3.3.co;2-6

Cited by 49 publications

(95 citation statements)

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“…At higher salt concentrations, the ability of the ions to affect the water structure is the more dominating factor. This is also in accordance with the description given by Curtis et al 10,11 The potential is often used to determine the pI of macromolecules or particulate systems, for characterization of the binding behavior of additives, and to estimate the colloidal stability of a system of interest. Solutions that are characterized by potentials > 30 mV (either positive or negative) are generally regarded as stable.…”

Section: Resultsmentioning

confidence: 99%

Study of the Solubility of a Modified Bacillus licheniformis α-Amylase around the Isoelectric Point

et al. 2007

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The solubility of a modified recombinant Bacillus licheniformis R-amylase (mBLA) has been studied by batch crystallization. A semi-pure preparation was chosen containing five isoforms with pI values from 6 to 7.3 (weighted average of 6.6). Small amounts (<1 %) of protein impurities were also present. Solubility was studied in the pH range of 6 to 8. The lowest solubility without added salts was 60 mg‚mL -1 at pH 7. The addition of 0.1 mol‚L -1 sodium salts of nitrate, sulfate, and thiocyanate had a small effect on solubility. However, solubility was lowered significantly by adding 0.5 mol‚L -1 sodium sulfate at all pH values and increased with 0.5 mol‚L -1 sodium thiocyanate at pH 7 and pH 8. The effect of anions on R-amylase solubility followed the Hofmeister series, and only weak evidence of reversal was seen below the isoelectric point. Cations had little effect on solubility. The sign and magnitude of the R-amylase potential was determined in the presence and absence of 0.1 mol‚L -1 salt. Qualitatively, potential correctly predicted the different salts influence on mBLA solubility.

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Section: Resultsmentioning

confidence: 99%

Study of the Solubility of a Modified Bacillus licheniformis α-Amylase around the Isoelectric Point

et al. 2007

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“…7 is favored), and (2) increase in the possibility for hydrophobic surface patches of two aggregating proteins to come closer. Salting-out effect is related to attractive proteinprotein interaction arising from preferential exclusion of the salt from protein-surface and consequent increase of proteinsurface free energy (40). Evidently, all these effects go beyond charge screening and DLVO model and are not separable.…”

Section: Kinetic Modelling Of the Oligomer Formationmentioning

confidence: 99%

Aggregation Stability of a Monoclonal Antibody During Downstream Processing

et al. 2011

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“…Forces involved in PPI include specific and non-specific interactions: hydrogen bonding, van der Waals interactions and steric interactions that have been suggested to play minor roles in dilute solutions of proteins in their native states. Additionally, electrostatic and hydrophobic interactions are considered to play major roles [46,47]. In cases where high concentrations of proteins exist in solutions, however, the relative contribution of these forces would be different [48].…”

Section: Association Of Protein Molecules: Amorphous Aggregationmentioning

confidence: 99%

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

Ebrahim‐Habibi

Morshedi

Rezaei‐Ghaleh

et al. 2010

JICS

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Protein aggregates, whether amorphous or structured (amyloid), have attracted much attention in recent years and despite extensive efforts, the mechanism of their formation is poorly understood. While "natural" aggregation (polymerization) of monomers could improve the biological function of some proteins, it is usually the darker side of this phenomenon which is discussed in many studies: deleterious aggregation that could lead to loss of biological activity under in vitro conditions or cause misfolding diseases. In this review, protein aggregation has been overviewed, starting from some general concepts involved in its formation, followed by mentioning studies aimed at elucidation of its kinetics and mechanism, or characterization of intermediates that would be aggregation-prone, and finally, reporting some of the studies related to the design of methods that would control the process. Similarly, amyloid aggregates have been defined, and current methods used in their characterization have been briefly described, with an emphasis on in silico studies. Finally, identification and design of such molecules which may be effective in control of this process is discussed.

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Protein‐protein and protein‐salt interactions in aqueous protein solutions containing concentrated electrolytes

Cited by 49 publications

References 0 publications

Study of the Solubility of a Modified Bacillus licheniformis α-Amylase around the Isoelectric Point

Study of the Solubility of a Modified Bacillus licheniformis α-Amylase around the Isoelectric Point

Aggregation Stability of a Monoclonal Antibody During Downstream Processing

Protein-Protein interactions leading to aggregation: Perspectives on mechanism, significance and control

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