Proteins and polyelectrolytes: A charged relationship

Becker, Alisa L.; Henzler, Katja; Welsch, Nicole; Ballauff, Matthias; Borisov, Oleg V.

doi:10.1016/j.cocis.2011.10.001

Cited by 108 publications

(112 citation statements)

References 47 publications

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“…2(b)), i.e., the mass of the complexes increases as C INS increases. As protein concentration increases each polyelectrolyte chain interacts with an increasing number of protein molecules, the degree of charge neutralization becomes higher and the size distribution of the complexes decreases, especially at the highest ionic strength (Becker et al, 2012). In contrast I 90 (or the mass of the complexes) shows a more steep increase in the case of PBS solutions, although the protein concentration range studied in these systems is wider due to the absence of coacervation.…”

Section: Physicochemical Characterization Of Qnphoseo:ins Complexes Imentioning

confidence: 96%

“…Polyelectrolyte block copolymers constitute an intriguing class of bio-inspired macromolecules, as they combine the structural properties of amphiphilic block copolymers, polyelectrolytes and surfactants and provide various possibilities for use as delivery nanosystems of genes and proteins through electrostatic complexation (Al-Tahami and Singh, 2007;Hartig et al, 2007;Pispas, 2007;Reis et al, 2008;Karayianni et al, 2011;Karayianni and Pispas, 2012;Becker et al, 2012;Haladjova et al, 2012;Varkouhi et al, 2012). Polymeric delivery systems based on nanoparticles have emerged as a promising approach for insulin delivery.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Complexation of cationic-neutral block polyelectrolyte with insulin and in vitro release studies

Pippa

Karayianni

Pispas

et al. 2015

International Journal of Pharmaceutics

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Insulin (INS) was incorporated into complexes with the block polyelectrolyte quaternized poly[3,5-bis(dimethylaminomethylene)hydroxystyrene]-b-poly(ethylene oxide) (QNPHOSEO), which is a cationic-neutral block polyelectrolyte. Light scattering techniques are used in order to examine the size, the size distribution and the ζ-potential of the nanocarriers in aqueous and biological media, which are found to depend on the ratio of the components and the physicochemical parameters during and after complex preparation. Circular dichroism and infrared spectroscopy, employed to investigate the structure of the complexed INS, show no alteration of protein structure after complexation. In vitro release profiles of the entrapped protein are found to depend on the ratio of the components and the solution conditions used during preparation of the complexes.

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Section: Physicochemical Characterization Of Qnphoseo:ins Complexes Imentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Complexation of cationic-neutral block polyelectrolyte with insulin and in vitro release studies

Pippa

Karayianni

Pispas

et al. 2015

International Journal of Pharmaceutics

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“…While in general brush-like and hydrogel-like layers, e.g., polyethylene glycols, attached to the surface will repel proteins [28,29], using charged polymers will result in attraction when the appropriate charge is being used. The main driving force is the replacement of several counterions from the brush-layer into the solution medium upon complexation of the protein which makes it entropically favorable while the multiple opposite charges ensure strong binding ( Figure 3a) [30,31]. In order to remove the proteins from the surface, either changing the pH to remove any charge interactions is needed or extremely high concentrations of strongly coordinating counterions to overcome the entropic penalty for protein removal.…”

Section: Surface Assembled Electrostatic Structuresmentioning

confidence: 99%

Polymer Directed Protein Assemblies

Rijn

2013

Polymers

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Protein aggregation and protein self-assembly is an important occurrence in natural systems, and is in some form or other dictated by biopolymers. Very obvious influences of biopolymers on protein assemblies are, e.g., virus particles. Viruses are a multi-protein assembly of which the morphology is dictated by poly-nucleotides namely RNA or DNA. This "biopolymer" directs the proteins and imposes limitations on the structure like the length or diameter of the particle. Not only do these bionanoparticles use polymer-directed self-assembly, also processes like amyloid formation are in a way a result of directed protein assembly by partial unfolded/misfolded biopolymers namely, polypeptides. The combination of proteins and synthetic polymers, inspired by the natural processes, are therefore regarded as a highly promising area of research. Directed protein assembly is versatile with respect to the possible interactions which brings together the protein and polymer, e.g., electrostatic, v.d. Waals forces or covalent conjugation, and possible combinations are numerous due to the large amounts of different polymers and proteins available. The protein-polymer interacting behavior and overall morphology is envisioned to aid in clarifying protein-protein interactions and are thought to entail some interesting new functions and properties which will ultimately lead to novel bio-hybrid materials.

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“…As a consequence, polymers take shrunk conformation and only weak interaction acts between polymer chains and the surface [43]. Both effects will bring about the smooth rearrangement of attached polymer chains on the surface [44].…”

Section: Resultsmentioning

confidence: 98%

Initial stage dynamics of bridging flocculation of polystyrene latex particles with low charge density polycation in a mixing flow near the isoelectric point

Kobayashi

Adachi

2015

Colloid Polym Sci

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Dynamics of ortho-kintetic flocculation of PSL particles with long-chain polycation of low charge density was studied together with the adsorption process of polyelectrolyte near isoelectric point as a function of ionic strength. Within the range of investigation, the initial rate of flocculation was found to take the maximum value immediately after the onset of mixing, but the flocculation gradually slows down with the progress of adsorption. The initial rate of flocculation goes through the minimum as ionic strength increases. Without salt addition, the rate of flocculation is about three times faster than that of salt-induced rapid coagulation. With slightly increasing ionic strength the rate of flocculation slows down because of the reductions of the stiffness and the size of polymer coil in solution and also of the smooth rearrangement of adsorbed chains. The adsorption process monitored by the electrophoresis demonstrates that the zero mobility appears much earlier than the time predicted by collision process in the presence of salt (KCl 100 mM). This trend can be explained by the concept of electrokinetically stagnant layer and by smooth spreading of polyelectrolyte on the colloidal surface. The kinetics of adsorption is in good accordance with the change in the flocculation rate.

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Proteins and polyelectrolytes: A charged relationship

Cited by 108 publications

References 47 publications

Complexation of cationic-neutral block polyelectrolyte with insulin and in vitro release studies

Complexation of cationic-neutral block polyelectrolyte with insulin and in vitro release studies

Polymer Directed Protein Assemblies

Initial stage dynamics of bridging flocculation of polystyrene latex particles with low charge density polycation in a mixing flow near the isoelectric point

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