43 research outputs found
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Mesophase Separation and Probe Dynamics in Protein-Polyelectrolyte Coacervates
Protein–polyelectrolyte coacervates are self-assembling macroscopically monophasic biomacromolecular fluids whose unique properties arise from transient heterogeneities. The structures of coacervates formed at different conditions of pH and ionic strength from poly(dimethyldiallylammonium chloride) and bovine serum albumin (BSA), were probed using fluorescence recovery after photobleaching. Measurements of self-diffusion in coacervates were carried out using fluorescein-tagged BSA, and similarly tagged Ficoll, a non-interacting branched polysaccharide with the same size as BSA. The results are best explained by temporal and spatial heterogeneities, also inferred from static light scattering and cryo-TEM, which indicate heterogeneous scattering centers of several hundred nm. Taken together with previous dynamic light scattering and rheology studies, the results are consistent with the presence of extensive dilute domains in which are embedded partially interconnected 50–700 nm dense domains. At short length scales, protein mobility is unobstructed by these clusters. At intermediate length scales, proteins are slowed down due to tortuosity effects within the blind alleys of the dense domains, and to adsorption at dense/dilute domain interfaces. Finally, at long length scales, obstructed diffusion is alleviated by the break-up of dense domains. These findings are discussed in terms of previously suggested models for protein–polyelectrolyte coacervates. Possible explanations for the origin of mesophase separation are offered
Multiple Scale Reorganization of Electrostatic Complexes of PolyStyrene Sulfonate and Lysozyme
We report on a SANS investigation into the potential for these structural
reorganization of complexes composed of lysozyme and small PSS chains of
opposite charge if the physicochemical conditions of the solutions are changed
after their formation. Mixtures of solutions of lysozyme and PSS with high
matter content and with an introduced charge ratio [-]/[+]intro close to the
electrostatic stoichiometry, lead to suspensions that are macroscopically
stable. They are composed at local scale of dense globular primary complexes of
radius ~ 100 {\AA}; at a higher scale they are organized fractally with a
dimension 2.1. We first show that the dilution of the solution of complexes,
all other physicochemical parameters remaining constant, induces a macroscopic
destabilization of the solutions but does not modify the structure of the
complexes at submicronic scales. This suggests that the colloidal stability of
the complexes can be explained by the interlocking of the fractal aggregates in
a network at high concentration: dilution does not break the local aggregate
structure but it does destroy the network. We show, secondly, that the addition
of salt does not change the almost frozen inner structure of the cores of the
primary complexes, although it does encourage growth of the complexes; these
coalesce into larger complexes as salt has partially screened the electrostatic
repulsions between two primary complexes. These larger primary complexes remain
aggregated with a fractal dimension of 2.1. Thirdly, we show that the addition
of PSS chains up to [-]/[+]intro ~ 20, after the formation of the primary
complex with a [-]/[+]intro close to 1, only slightly changes the inner
structure of the primary complexes. Moreover, in contrast to the synthesis
achieved in the one-step mixing procedure where the proteins are unfolded for a
range of [-]/[+]intro, the native conformation of the proteins is preserved
inside the frozen core
Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene
We have studied the formation and the stability of grafted block complex coacervate core micelles (C3Ms) in solution and the influence of grafted block C3M coatings on the adsorption of the proteins β-lactoglobulin, bovine serum albumin, and lysozyme. The C3Ms consist of a grafted block copolymer PAA21-b-PAPEO14 (poly(acrylic acid)-b-poly(acrylate methoxy poly(ethylene oxide)), with a negatively charged PAA block and a neutral PAPEO block and a positively charged homopolymer P2MVPI (poly(N-methyl 2-vinyl pyridinium iodide). In solution, these C3Ms partly disintegrate at salt concentrations between 50 and 100 mM NaCl. Adsorption of C3Ms and proteins has been studied with fixed-angle optical reflectometry, at salt concentrations ranging from 1 to 100 mM NaCl. In comparison with the adsorption of PAA21-b-PAPEO14 alone adsorption of C3Ms significantly increases the amount of PAA21-b-PAPEO14 on the surface. This results in a higher surface density of PEO chains. The stability of the C3M coatings and their influence on protein adsorption are determined by the composition and the stability of the C3Ms in solution. A C3M-PAPEO14/P2MVPI43 coating strongly suppresses the adsorption of all proteins on silica and polystyrene. The reduction of protein adsorption is the highest at 100 mM NaCl (>90%). The adsorbed C3M-PAPEO14/P2MVPI43 layer is partly removed from the surface upon exposure to an excess of β-lactoglobulin solution, due to formation of soluble aggregates consisting of β-lactoglobulin and P2MVPI43. In contrast, C3M-PAPEO14/P2MVPI228 which has a fivefold longer cationic block enhances adsorption of the negatively charged proteins on both surfaces at salt concentrations above 1 mM NaCl. A single PAA21-b-PAPEO14 layer causes only a moderate reduction of protein adsorption
Role of Polyelectrolyte Persistence Length in the Binding of Oppositely Charged Micelles, Dendrimers, and Protein to Chitosan and Poly(dimethyldiallyammonium chloride)
Influence of Chain Stiffness on the Interaction of Polyelectrolytes with Oppositely Charged Micelles and Proteins â€
Rheology and Gelation of Hyaluronic Acid/Chitosan Coacervates
Hyaluronic acid (HA) and chitosan (CHI) are biopolyelectrolytes which are interesting for both the medical and polymer physics communities due to their biocompatibility and semi-flexibility, respectively. In this work, we demonstrate by rheology experiments that the linear viscoelasticity of HA/CHI coacervates depends strongly on the molecular weight of the polymers. Moduli for coacervates were found significantly higher than those of individual HA and CHI physical gels. A remarkable 1.5-fold increase in moduli was noted when catechol-conjugated HA and CHI were used instead. This was attributed to the conversion of coacervates to chemical gels by oxidation of 3,4-dihydroxyphenylalanine (DOPA) groups in HA and CHI to di-DOPA crosslinks. These rheological results put HA/CHI coacervates in the category of strong candidates as injectable tissue scaffolds or medical adhesives