Interaction protein-polyelectrolyte

Polyelectrolyte complexes formed by polyion pairing are of special interest, including protein-polyelectrolyte interactions such as protein-DNA complexes. A special case of polyelectrolyte complexes are polyelectrolyte multilayers (PEM) on surfaces formed by ion pairing, van der Waals interactions and counterion release of oppositely charged polyelectrolytes [2, 3]. 

The matrix polyelectrolyte capsules have high protein-loading capacity, and both the loading and, in principle, the release are driven by electrostatic interaction with polyelectrolytes [111]. Moreover, the loading and release can be controlled by the number of polyelectrolyte adsorption steps [112] as well as by the pore size of the CaCC>3 cores [116],... 

Analyses of phase boundaries reveal evidence for polymer saturation in the presence of excess protein. Phase boundaries also facilitate comparisions of the behavior of various proteins. The failure of net surface charge density as a universal parameter for protein-polyelectrolyte interaction is believed to be related to the existence of "charge patches" on the protein surface. The determination of a more realistic protein charge parameter possesses great importance, since the ionic interactions of proteins are exploited in a variety of applications, including protein purification via ion exchange liquid chromatography. 

Protein Interaction between polyelectrolytes and proteins results in formation... 

Kayitmazer, A. B., Seyrec, E., Dubin, P. L., and Staggemeier, B. A. 2003. Influence of chain stiffness on the interaction of polyelectrolytes with oppositely charged micelles and proteins. J. Phys. Chem. B. 107 8158-8165. 

Exploring Cell Interactions of Dendritic and Protein Polyelectrolytes... 

Ladam G, et al. Protein interactions with polyelectrolyte multilayers interactions between human serum albumin and polystyrene sulfonate/polyaUylamine multilayers. Biomacromolecules 2000 1(4) 674—87. 

PAA is a typical weak polyacid and has been widely used as a model to investigate protein-polyelectrolyte interactions. BallaulTs group systematically studied BSA adsorption on so-called "spherical polyelectrolyte brushes" (SPBs) consisting of a polystyrene (PS) core covered with PAA brushes (as shown in Figure 7.4)... 

Simulating complex systems, cell, combustion, polyelectrolytes and complex fluids, atmospheres, hydrogeology, catalysts under industrial conditions, drug design, protein-DNA interactions, protein-protein, RNA folding, protein folding, metabolic networks, conformational sampling... 

The adsorption of DNA films assembled from oligonucleotides composed of two homopolymeric diblocks (polyA G and polyTnCn) were studied in the presence of salt. The growth of fihn increased with salt concentration [22]. The studies on polyelectrolyte complexation have offered wide applications such as water treatment, surface modification, dmg delivery system, tissue engineering. To understand the formation of protein-polyelectrolyte complex is important due to the interaction between polyanions or polycations with protein macromolecules or polyelectrolytes. Soluble complexes can be formed and amphorous can be precipitated with the interaction of molecules. Complex formation is generally performed in the bulk solutions. Potentiometry, conductometry, viscosimetry, turbidimetry, or electrophoretic and quasi-elastic light scattering are used to follow... 

A wide variety of synthetic and natural PE can interact with globular proteins to form stable protein-polyelectrolyte complexes (PE-P) that result in the formation of soluble or non-soluble complexes [5, 47]. The non-soluble complex can be easily separated by centrifugation or simple decantation. Precipitation as a concentration step offers several advantages in that it is easy to scale up, uses simple equipment and can be based on a large variety of alternative precipitants. When PE-P is specifically formed with one of the proteins in the crude extract followed by a phase separation, the process could be used as a convenient strategy for the isolation and purification of the target protein [8]. 

Boeris, V., et al. Protein-flexible chain polymer interactions to explain protein partition in aqueous two-phase systems and the protein-polyelectrolyte complex formation. Int. J. Biol. Macromol. 41(3), 286-294 (2007)... 

High sorption capacities with respect to protein macromolecules are observed when highly permeable macro- and heteroreticular polyelectrolytes (biosorbents) are used. In buffer solutions a typical picture of interaction between ions with opposite charges fixed on CP and counterions in solution is observed. As shown in Fig. 13, in the acid range proteins are not bonded by carboxylic CP because the ionization of their ionogenic groups is suppressed. The amount of bound protein decreases at high pH values of the solution because dipolar ions proteins are transformed into polyanions and electrostatic repulsion is operative. The sorption maximum is either near the isoelectric point of the protein or depends on the ratio of the pi of the protein to the pKa=0 5 of the carboxylic polyelectrolyte [63]. It should be noted that this picture may be profoundly affected by the mechanism of interaction between CP and dipolar ions similar to that describedby Eq. (3.7). 

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