Controlling Phase Separation of Lysozyme with Polyvalent Anions

Bye, Jordan W.; Curtis, Robin

doi:10.1021/acs.jpcb.8b10868

Cited by 32 publications

(68 citation statements)

References 94 publications

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“…This behavior is analogous to the reentrant condensation phase behavior of proteins in the presence of multivalent counterions. 51 , 52 Protein encapsulation is currently a topic of intense development 35 , 50 , 79 , 80 and macrocycle-masking may be a simple approach to tackle this challenge.…”

Section: Discussionmentioning

confidence: 99%

Facile Fabrication of Protein–Macrocycle Frameworks

et al. 2021

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Precisely defined protein aggregates, as exemplified by crystals, have applications in functional materials. Consequently, engineered protein assembly is a rapidly growing field. Anionic calix[n]arenes are useful scaffolds that can mold to cationic proteins and induce oligomerization and assembly. Here, we describe protein-calixarene composites obtained via cocrystallization of commercially available sulfonato-calix[8]arene ( sclx 8 ) with the symmetric and “neutral” protein RSL. Cocrystallization occurred across a wide range of conditions and protein charge states, from pH 2.2–9.5, resulting in three crystal forms. Cationization of the protein surface at pH ∼ 4 drives calixarene complexation and yielded two types of porous frameworks with pore diameters >3 nm. Both types of framework provide evidence of protein encapsulation by the calixarene. Calixarene-masked proteins act as nodes within the frameworks, displaying octahedral-type coordination in one case. The other framework formed millimeter-scale crystals within hours, without the need for precipitants or specialized equipment. NMR experiments revealed macrocycle - modulated side chain p K a values and suggested a mechanism for pH-triggered assembly. The same low pH framework was generated at high pH with a permanently cationic arginine-enriched RSL variant. Finally, in addition to protein framework fabrication, sclx 8 enables de novo structure determination.

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Section: Discussionmentioning

confidence: 99%

Facile Fabrication of Protein–Macrocycle Frameworks

et al. 2021

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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%

“…[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]). Also shown is the conductivity scale for pure NaCl aqueous solution.…”

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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“…[258] Remarkably, a protein crystallisation strategy similar to the one demonstrated by Zhang et al [19] has been pursued using negative multivalent ion complexes. [24][25][26]259] Reentrant Condensation. The inversion of the surface charge is related to a specific phase behaviour called reentrant condensation known from polyelectrolytes (see, e. g., Ref.…”

Section: Lanthanide-induced Phase Behaviour In Protein Solutionsmentioning

confidence: 99%

Multivalent ions and biomolecules: Attempting a comprehensive perspective

2020

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Ions are ubiquitous in nature. They play a key role for many biological processes on the molecular scale, from molecular interactions, to mechanical properties, to folding, to self‐organisation and assembly, to reaction equilibria, to signalling, to energy and material transport, to recognition etc. Going beyond monovalent ions to multivalent ions, the effects of the ions are frequently not only stronger (due to the obviously higher charge), but qualitatively different. A typical example is the process of binding of multivalent ions, such as Ca2+, to a macromolecule and the consequences of this ion binding such as compaction, collapse, potential charge inversion and precipitation of the macromolecule. Here we review these effects and phenomena induced by multivalent ions for biological (macro)molecules, from the “atomistic/molecular” local picture of (potentially specific) interactions to the more global picture of phase behaviour including, e. g., crystallisation, phase separation, oligomerisation etc. Rather than attempting an encyclopedic list of systems, we rather aim for an embracing discussion using typical case studies. We try to cover predominantly three main classes: proteins, nucleic acids, and amphiphilic molecules including interface effects. We do not cover in detail, but make some comparisons to, ion channels, colloidal systems, and synthetic polymers. While there are obvious differences in the behaviour of, and the relevance of multivalent ions for, the three main classes of systems, we also point out analogies. Our attempt of a comprehensive discussion is guided by the idea that there are not only important differences and specific phenomena with regard to the effects of multivalent ions on the main systems, but also important similarities. We hope to bridge physico‐chemical mechanisms, concepts of soft matter, and biological observations and connect the different communities further.

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Controlling Phase Separation of Lysozyme with Polyvalent Anions

Cited by 32 publications

References 94 publications

Facile Fabrication of Protein–Macrocycle Frameworks

Facile Fabrication of Protein–Macrocycle Frameworks

Protein dielectrophoresis: Key dielectric parameters and evolving theory

Multivalent ions and biomolecules: Attempting a comprehensive perspective

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