High pressure stability of protein complexes studied by static and dynamic light scattering

Gebhardt, Ronald; Kulozik, Ulrich

doi:10.1080/08957959.2010.543900

Cited by 3 publications

(2 citation statements)

References 17 publications

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“…Elevated pressure may promote either the formation or dissociation of aggregates or other macromolecular assemblies, depending on which process results in the lower partial specific molar volume of the species. − For example, the high pressure dissociation process was demonstrated using the Enterobacteria phage P22 tailspike aggregates to create partially unfolded monomers . Another study showed pressure-induced aggregation of an interleukin-1 protein .…”

Section: Introductionmentioning

confidence: 99%

High Pressure Light Scattering of Therapeutic Proteins To Probe Aggregation and Protein–Protein Interactions

et al. 2023

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There is interest in the direct in situ measurement of protein aggregation and reversible protein–protein interactions at high pressure as a means to assess protein stability. This is currently limited by the availability of in-house analytical methods. High-pressure (HP) scattering instrumentation (using either neutrons, X-rays, or light sources) are relatively rare, due to extensive development hurdles and lack of standardization. This report focuses on design, operation, and application of a new HP light scattering apparatus based on commercially available equipment with a view to wider applications. HP static light scattering results were obtained for two monoclonal antibodies (MAbs) that exhibit different extents of unfolding and aggregation at these conditions. Aggregation that was observed during in situ pressure incubations varied by MAb and total ionic strength of solution. This was conducted in tandem with ex situ measurements on MAb solutions that were incubated under pressure, where monomer loss was measured with size exclusion chromatography. Pressure cycling was also used to assess the extent of pressure-induced reversible and irreversible aggregation. Finally, the ability of the HP light scattering apparatus to assess the influence of pressure on reversible protein–protein interactions in the canonical sense of second osmotic virial coefficients was assessed using lysozyme, a relatively well-characterized protein under hydrostatic pressure. The method offers a convenient and reproducible capability that complements current small angle neutron/X-ray instrumentation, providing measurements that can be used to optimize the planning and interpretation of scattering data from synchrotron or neutron research facilities. Our results address a growing demand to characterize protein aggregates and aggregation-prone partially unfolded intermediates.

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Section: Introductionmentioning

confidence: 99%

High Pressure Light Scattering of Therapeutic Proteins To Probe Aggregation and Protein–Protein Interactions

et al. 2023

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“…For instance, it was shown that the pressure dissociation of casein micelles shifted by 200 MPa towards higher pressures after addition of 0.1 M calcium chloride [ 12 , 13 ]. For other processes, pressure can take over the role of salt ions.…”

Section: Introductionmentioning

confidence: 99%

The Combined Effect of High Hydrostatic Pressure and Calcium Salts on the Stability, Solubility and Gel Formation of β-Lactoglobulin

Saalfeld

Riegel

Kulozik

et al. 2015

Foods

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Stability, aggregation and gelation of β-Lactoglobulin are affected by high pressure and salts of the Hofmeister series. Little is known about their combined effects on structure formation processes of β-Lactoglobulin, mainly because many salts of the series are not suitable for use in food. Here, we investigate the effect of calcium salts on the strength of pressure-induced gels, inspired by the fact that high pressure and salts change the water structure in a similar way. We find that the larger the applied pressures, the higher the strength of the gels. In addition to pressure, there is a significant influence by the type of anions and the amount of added calcium salts. Gel strength increases in the order CaCl2 < Ca (NO3)2 < CaI2. This trend correlates with the position of the salts in the Hofmeister series. The results are explained by analogy with the thermal aggregate formation by taking reaction rates for unfolding and aggregation, as well as specific/non-specific salts effect into consideration.

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High-pressure effect on the dynamics of solvated peptides

Nellas

Glover

Hamelberg

et al. 2012

The Journal of Chemical Physics

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The dynamics of peptides has a direct connection to how quickly proteins can alter their conformations. The speed of exploring the free energy landscape depend on many factors, including the physical parameters of the environment, such as pressure and temperature. We performed a series of molecular dynamics simulations to investigate the pressure-temperature effects on peptide dynamics, especially on the torsional angle and peptide-water hydrogen bonding (H-bonding) dynamics. Here, we show that the dynamics of the omega angle and the H-bonding dynamics between water and the peptide are affected by pressure. At high temperature (500 K), both the dynamics of the torsional angle ω and H-bonding slow down significantly with increasing pressure, interestingly, at approximately the same rate. However, at a lower temperature of 300 K, the observed trend on H-bonding dynamics as a function of pressure reverses, i.e., higher pressure speeds up H-bonding dynamics.

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High pressure stability of protein complexes studied by static and dynamic light scattering

Cited by 3 publications

References 17 publications

High Pressure Light Scattering of Therapeutic Proteins To Probe Aggregation and Protein–Protein Interactions

High Pressure Light Scattering of Therapeutic Proteins To Probe Aggregation and Protein–Protein Interactions

The Combined Effect of High Hydrostatic Pressure and Calcium Salts on the Stability, Solubility and Gel Formation of β-Lactoglobulin

High-pressure effect on the dynamics of solvated peptides

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