Complexation of trypsin and alcohol dehydrogenase with poly(diallyldimethylammonium chloride)

Xia, Jiliang; Mattison, Kevin; Romano, Vincent; Dubin, Paul L.; Muhoberac, Barry B.

doi:10.1002/(sici)1097-0282(19970405)41:4<359::aid-bip1>3.0.co;2-l

Cited by 57 publications

(59 citation statements)

References 23 publications

(4 reference statements)

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“…The qualitative nature of turbidity-style measurements allows a phenomenological characterization of coacervate phase behavior, rather than a more direct quantification of the binodal phase space [8,15,71,[73][74][75][76][77]83,88,[91][92][93]104,105,108,112,114,. Typical characterization experiments include evaluation of the stoichiometric ratio of polycation to polyanion, the effect of increasing salt concentration, and the effect of variable pH.…”

Section: Connecting Coacervate Phase Behavior With Materials Dynamicsmentioning

confidence: 99%

Linear viscoelasticity of complex coacervates

Liu

Winter

Perry

2017

Advances in Colloid and Interface Science

125

163

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Rheology is a powerful method for materials characterization that can provide detailed information about the self-assembly, structure, and intermolecular interactions present in a material. Here, we review the use of linear viscoelastic measurements for the rheological characterization of complex coacervate-based materials. Complex coacervation is an electrostatically and entropically-driven associative liquid-liquid phase separation phenomenon that can result in the formation of bulk liquid phases, or the self-assembly of hierarchical, microphase separated materials. We discuss the need to link thermodynamic studies of coacervation phase behavior with characterization of material dynamics, and provide parallel examples of how parameters such as charge stoichiometry, ionic strength, and polymer chain length impact self-assembly and material dynamics. We conclude by highlighting key areas of need in the field, and specifically call for the development of a mechanistic understanding of how molecular-level interactions in complex coacervate-based materials affect both selfassembly and material dynamics.

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Section: Connecting Coacervate Phase Behavior With Materials Dynamicsmentioning

confidence: 99%

Linear viscoelasticity of complex coacervates

Liu

Winter

Perry

2017

Advances in Colloid and Interface Science

125

163

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“…Another attractive feature of this "soft method" is that protein stability and bioactivity can be retained during the separation process. 10 PE/protein complex coacervation is a liquid−liquid phase separation occurring through nonspecific electrostatic interactions. For protein−PE systems, the protein charge density is pH-dependent, and a critical pH marks the onset of binding of proteins to polymer chains.…”

Section: ■ Introductionmentioning

confidence: 99%

Protein-Selective Coacervation with Hyaluronic Acid

Du¹,

Dubin²,

Hoagland³

et al. 2014

Biomacromolecules

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Selective coacervation with hyaluronic acid (HA), a biocompatible and injectable anionic polysaccharide, was used to isolate a target protein, bovine serum albumin (BSA), with 90% purity from a 1:1 mixture with a second protein of similar pI, β-lactoglobulin (BLG). This separation was attributed to the higher HA-affinity of BSA, arising from its more concentrated positive domain. The values of pH corresponding respectively to the onset of complex formation, coacervation, precipitation, and redissolution (pH(c), pHϕ, pH(p), and pH(d)) were determined as a function of ionic strength I. These pH values were related to critical values of protein charge, Z, and their dependence on I provided some insights into the mechanisms of these transitions. The higher polyanion binding affinity of BSA, deduced from its higher values of pH(c), was confirmed by isothermal titration calorimetry (ITC). Confocal laser microscopy clearly showed time-dependent coalescence of vesicular droplets into a continuous film. Comparisons with prior results for the polycation poly(diallyldimethylammonium chloride) (PDADMAC) show reversal of protein selectivity due to reversal of the polyelectrolyte charge. Stronger binding of both proteins to PDADMAC established by ITC may be related to the higher chain flexibility and effective linear charge density of this polycation.

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“…HS-protein interaction may lead to modification of the protein structure and, consequently, to a change in its biological activity. The extent to which this occurs depends on the specific conditions (Brouwer et al, 1990;Wen and Dubin, 1997;Xia et al, 1997). Furthermore, binding to other substances makes proteins less susceptible to microbial degradation and this can be environmentally hazardous.…”

Section: Introductionmentioning

confidence: 99%