Interactions of hydrophobically modified poly(sodium acrylate) with globular proteins
| Autor: | F. Petit, R. Audebert, Ilias Iliopoulos |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
Polymers and Plastics biology Chemistry Globular protein Cationic polymerization Polyelectrolyte Hydrophobic effect Colloid and Surface Chemistry Pulmonary surfactant Polymer chemistry Materials Chemistry biology.protein Organic chemistry Physical and Theoretical Chemistry Bovine serum albumin Alkyl Macromolecule |
| Zdroj: | Colloid & Polymer Science. 273:777-781 |
| ISSN: | 1435-1536 0303-402X |
| DOI: | 10.1007/bf00658756 |
| Popis: | 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 investigated at pH=9 by rheology and to a lesser extent by steady-state fluorescence spectroscopy. Under suitable concentration conditions, this association leads to a drastic viscosity enhancement which is improved when the polymer hydrophobicity is increased. A mechanism is proposed: the hydrophobic regions of the globular proteins interact strongly with the alkyl groups of one or more polymer chains. In the later case, the macromolecules are crosslinked via the proteins, which leads to viscosity enhancement and even gelation. Analogies and differences between these systems and surfactant/HMPA systems previously studied in our laboratory are emphasized and discussed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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