Complex Formation between Bovine Serum Albumin and Strong Polyelectrolytes: Effect of Polymer Charge Density
| Autor: | Kevin W. Mattison, Isabelle J. Brittain, Paul L. Dubin |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
chemistry.chemical_classification
Chromatography biology Charge density Polymer Polyelectrolyte Surfaces Coatings and Films Crystallography chemistry.chemical_compound Sulfonate chemistry Ionic strength Materials Chemistry Copolymer biology.protein Titration Physical and Theoretical Chemistry Bovine serum albumin |
| Zdroj: | The Journal of Physical Chemistry B. 102:3830-3836 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/jp980486u |
| Popis: | Light scattering and pH titration were used to examine the binding of bovine serum albumin (BSA) to poly(diallyldimethylammonium chloride) (PDADMAC), poly(acrylamidomethylpropyl sulfonate) (PAMPS), poly(methacrylamidopropyltrimethylammonium chloride) (PMAPTAC), and an AMPS−acrylamide random copolymer (PAMPS80AAm20). The critical protein charge required to induce protein−polyelectrolyte complexation, (Zpr)c, was found to vary linearly with the square root of the ionic strength (I1/2), i.e., with the Debye−Huckel parameter (κ), the proportionality constant being a function of polyelectrolyte chain parameters such as intrinsic stiffness and charge density. This linearity was remarkably continuous through Zpr = 0, with (Zpr)c occurring predominantly “on the wrong side” of the isoionic point; i.e., the onset of binding was typically observed when the global protein charge was of the same sign as the polyelectrolyte. Binding of BSA to the lower charge density polyanion (PAMPS80AAm20) unexpectedly occurred under... |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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