The electrokinetic potential of therapeutic proteins and its modulation: Impact on protein stability

Wagner, Michael R.; Reiche, Katharina; Blume, Alfred; Garidel, Patrick

doi:10.1016/j.colsurfa.2012.09.024

Cited by 18 publications

(15 citation statements)

References 55 publications

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“…The effect of pH on protein aggregation can be explained to first approximation by invoking DLVO theory of colloid science [167][168][169] based on the balance of attractive (van der Waals) and repulsive (Coulomb) interactions. This can only provide a rough guide since ion specificity is not included.…”

Section: Protein Aggregation Explained By Specific Ion Bindingmentioning

confidence: 99%

Models and mechanisms of Hofmeister effects in electrolyte solutions, and colloid and protein systems revisited

2014

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Specific effects of electrolytes have posed a challenge since the 1880's. The pioneering work was that of Franz Hofmeister who studied specific salt induced protein precipitation. These effects are the rule rather the exception and are ubiquitous in chemistry and biology. Conventional electrostatic theories (Debye-Hückel, DLVO, etc.) cannot explain such effects. Over the past decades it has been recognised that additional quantum mechanical dispersion forces with associated hydration effects acting on ions are missing from theory. In parallel Collins has proposed a phenomenological set of rules (the law of matching water affinities, LMWA) which explain and bring to order the order of ion-ion and ion-surface site interactions at a qualitative level. The two approaches appear to conflict. Although the need for inclusion of quantum dispersion forces in one form or another is not questioned, the modelling has often been misleading and inappropriate. It does not properly describe the chemical nature (kosmotropic/chaotropic or hard/soft) of the interacting species. The success of the LMWA rules lies in the fact that they do. Here we point to the way that the two apparently opposing approaches might be reconciled. Notwithstanding, there are more challenges, which deal with the effect of dissolved gas and its connection to 'hydrophobic' interactions, the problem of water at different temperatures and 'water structure' in the presence of solutes. They take us to another dimension that requires the rebuilding of theoretical foundations.

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Section: Protein Aggregation Explained By Specific Ion Bindingmentioning

confidence: 99%

Models and mechanisms of Hofmeister effects in electrolyte solutions, and colloid and protein systems revisited

2014

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“…Proteins represent a class of electrolyte, and as sketched in Fig. 5 [39–41] exhibit a zeta‐potential value (also known as the electrochemical potential) that is dependent on the pH and ionic strength of the aqueous solvent. These are characteristics recognized to be associated with the presence of an electrical double layer [42,43].…”

Section: α‐Dispersion and Electrical Double Layermentioning

confidence: 99%

“…A) The zeta potential as a function of pH for BSA and lysozyme (based on Wagner et al. [39]). B) Zeta potential of a) 1 g/mL lysozyme (in 10 × 10 −3 m Tris at pH 9.0) versus ionic strength of added NaCl or citrate (based on Bye & Curtis [40]); b) 5% BSA (median particle size 178 nm) in 1 × 10 −3 m KCl versus added CaCl 2 (Dukhin and Parlia [41]).…”

Section: α‐Dispersion and Electrical Double Layermentioning

confidence: 99%

Protein dielectrophoresis: Key dielectric parameters and evolving theory

Hölzel

Pethig

2020

Electrophoresis

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Globular proteins exhibit dielectrophoresis (DEP) responses in experiments where the applied field gradient factor ∇E2 appears far too small, according to standard DEP theory, to overcome dispersive forces associated with the thermal energy kT of disorder. To address this a DEP force equation is proposed that replaces a previous empirical relationship between the macroscopic and microscopic forms of the Clausius–Mossotti factor. This equation relates the DEP response of a protein directly to the dielectric increment δε+ and decrement δε− that characterize its β‐dispersion at radio frequencies, and also indirectly to its intrinsic dipole moment by way of providing a measure of the protein's effective volume. A parameter Γpw, taken as a measure of cross‐correlated dipole interactions between the protein and its water molecules of hydration, is included in this equation. For 9 of the 12 proteins, for which an evaluation can presently be made, Γpw has a value of ≈4600 ± 120. These conclusions follow an analysis of the failure of macroscopic dielectric mixture (effective medium) theories to predict the dielectric properties of solvated proteins. The implication of a polarizability greatly exceeding the intrinsic value for a protein might reflect the formation of relaxor ferroelectric nanodomains in its hydration shell.

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“…As a limit between stable and unstable suspensions, ζ=±30 mV may be assumed [35]. However, zeta potential should not be used as a stand-alone predictive tool for the evaluation and optimization of colloidal stability, since other physical forces may be involved in this phenomenon [36].…”

Section: Evolution Of Average Size Of Ew Particlesmentioning

confidence: 99%

Power Ultrasound Assisted Design of Egg Albumin Nanoparticles

2015

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The objective of this work was to develop egg white (EW) nanoparticles by application of high intensity ultrasound (HIUS) at different solution pHs and treatment temperatures. At pH 7 HIUS without heating decreased the particle size. In contrast, the use of thermosonication (TS) increased the particle size. At pH 3, the application of both HIUS and TS induced a significant reduction of particle size. at pH 7 zeta potential did not vary significantly when native solutions were sonicated without heating; however a great decrease was observed when TS or heating were applied. At pH 3, sonication decreased the zeta potential of particles but TS or heating increased the charge. By applying TS (85°C, 20 min and pH 3) a bimodal distribution was obtained, including particles of 295 and 70 nm of diameter. At the same pH, without heating, a monomodal population of 220 nm of diameter was obtained.

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The electrokinetic potential of therapeutic proteins and its modulation: Impact on protein stability

Cited by 18 publications

References 55 publications

Models and mechanisms of Hofmeister effects in electrolyte solutions, and colloid and protein systems revisited

Models and mechanisms of Hofmeister effects in electrolyte solutions, and colloid and protein systems revisited

Protein dielectrophoresis: Key dielectric parameters and evolving theory

Power Ultrasound Assisted Design of Egg Albumin Nanoparticles

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