Rodlike complexes of a polyelectrolyte (hyaluronan) and a protein (lysozyme) observed by SANS.

@article{Morfin2011RodlikeCO,
  title={Rodlike complexes of a polyelectrolyte (hyaluronan) and a protein (lysozyme) observed by SANS.},
  author={Isabelle Morfin and Eric Buhler and Fabrice Cousin and Isabelle Grillo and François Bou{\'e}},
  journal={Biomacromolecules},
  year={2011},
  volume={12 4},
  pages={
          859-70
        }
}
We study by small-angle neutron scattering (SANS) the structure of hyaluronan -lysozyme complexes. Hyaluronan (HA) is a polysaccharide of 9 nm intrinsic persistence length that bears one negative charge per disaccharide monomer (M(mol) = 401.3 g/mol); two molecular weights, M(w) = 6000 and 500,000 Da were used. The pH was adjusted at 4.7 and 7.4 so that lysozyme has a global charge of +10 and +8, respectively. The lysozyme concentration was varied from 3 to 40 g/L at constant HA concentration… 

Structural behaviour of sodium hyaluronate in concentrated oppositely charged surfactant solutions.

Extended rod-like structures of the PESCs prevent molecular dissolution of HA by TTAB, and this effect was systematically studied in the concentration range from 1 to 25 mM HA.

The uncommon structures of oppositely charged hyaluronan/surfactant assemblies under physiological conditions.

Findings demonstrate that the HA network structure in solution basically remains unaffected by complexation with oppositely charged surfactant, explaining the unchanged rheological behavior, and the formation of unique PESC local "coacervate" structure within the HA hydrogel network.

Complexation of β-lactoglobulin fibrils and sulfated polysaccharides.

Fibrils of β-lactoglobulin, formed by heating at pH 2, were titrated with a sulfated polysaccharide (κ-carrageenan) to determine the morphology and mechanism of complex formation at low pH to describe the formation of spherical aggregates attached along the protein fibrils with increases in the carrageenan concentration.

Interpolyelectrolyte complexes based on hyaluronic acid-block-poly(ethylene glycol) and poly-L-lysine

The preparation of spherical, nanosized interpolyelectrolyte complexes by the interaction of hyaluronic acid-block-poly(ethylene glycol) (HA-b-PEG) with poly-L-lysine (PLL) at a stoichiometric

Complex coacervates of hyaluronic acid and lysozyme: effect on protein structure and physical stability.

Chitosan/alkylethoxy carboxylates: a surprising variety of structures.

The state of aggregation in these mixtures can be tuned structurally over quite a range only by rather small changes in pH, which is attractive for many potential applications.

Folding Behaviors of Protein (Lysozyme) Confined in Polyelectrolyte Complex Micelle.

The finding that lysozyme and a double hydrophilic block copolymer can form a polyelectrolyte complex micelle with a particle size of ∼30 nm provides an ideal water-soluble model system to study the important role of electrostatic interaction in the complexation between proteins and polymers, leading to important new knowledge on the protein-polymer interactions.

Tuning the solution organization of cationic polymers through interactions with bovine serum albumin.

The ability to tune the polyelectrolyte/protein interactions and polyelectralyte chain-chain associations by modifying the hydrophobic content of the polyElectrolytes is demonstrated.
...

References

SHOWING 1-10 OF 51 REFERENCES

Spatial structure and composition of polysaccharide-protein complexes from small angle neutron scattering.

The structure of lysozyme-pectin complexes is driven by electrostatic interactions and not by hydrophobic interactions, and the molecular weight also has a large influence on the structure of the complexes because long chains tend to form larger globules.

Microstructure of β-Lactoglobulin/Pectin Coacervates Studied by Small-Angle Neutron Scattering

Small-angle neutron scattering (SANS) has been used to investigate the microstructure of β-lactoglobulin/pectin coacervates prepared by different initial protein/polysaccharide weight ratio (r),

Complexation of Proteins with a Strong Polyanion in an Aqueous Salt-free System

We studied the formation in a salt-free solution of complexes between potassium poly(vinyl alcohol) sulfate (KPVS), a strong polyelectrolyte, and proteins with known amino-acid sequences:  papain,

Ionic strength dependence of protein-polyelectrolyte interactions.

Modelling of protein electrostatics via Delphi is used to visualize this effect for BSA, lysozyme, insulin, and beta-lactoglobulin, which appears to be a general effect caused by electrostatic repulsions that can coexist simultaneously with hydrophobic interactions.

Effects of protein-polyelectrolyte affinity and polyelectrolyte molecular weight on dynamic properties of bovine serum albumin-poly(diallyldimethylammonium chloride) coacervates.

Viscoelastic behavior indicated a tenuous network, solidlike at low strain but re-forming after breakage by shear, and high MW sensitivity was observed by rheology for the terminal time, which increased as well with the strength of polyelectrolyte-protein interaction.

Electrostatic interactions between hyaluronan and proteins at pH 4: how do they modulate hyaluronidase activity.

It is shown that at 0 and 150 mmol L(-1) NaCl, BSA competes with HAase in forming complexes with HA and thus induces HAase release resulting in a large increase in the hydrolysis rate.

Chain persistence length and structure in hyaluronan solutions: Ionic strength dependence for a model semirigid polyelectrolyte

In this study, we have directly determined for the first time the structure and the chain conformation of hyaluronan, a model semirigid polyelectrolyte polysaccharide. At high ionic strength,

Finite size and inner structure controlled by electrostatic screening in globular complexes of proteins and polyelectrolytes.

We present an extended structural study of globular complexes made by mixing a positively charged protein (lysozyme) and a negatively charged polyelectrolyte (PSS). We study the influence of all the

Interactions of hydrophobically modified poly(sodium acrylate) with globular proteins

The association of a series of hydrophobically modified poly(sodium acrylate) (HMPA) with lysozyme, a cationic globular protein, or with bovine serum albumin (BSA), an anionic globular protein, was
...