Chain length effects on electrostatic interactions between hyaluronan fragments and albumin
| Autor: | Brigitte Deschrevel, Jean-Claude Vincent, Hélène Lenormand |
|---|---|
| Přispěvatelé: | Transformations et Agro-ressources (UT&A), UniLaSalle, Polymères Biopolymères Surfaces (PBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Polymers and Plastics
Stereochemistry Kinetics Serum albumin 03 medical and health sciences 0302 clinical medicine Chain (algebraic topology) Materials Chemistry Molecule Solubility Bovine serum albumin Hyaluronan 030304 developmental biology 0303 health sciences Electrostatic interactions Aqueous solution biology Chemistry Chain length effect Organic Chemistry Polysaccharide–protein complex Polyelectrolyte [CHIM.POLY]Chemical Sciences/Polymers 030220 oncology & carcinogenesis Biophysics biology.protein |
| Zdroj: | Carbohydrate Polymers Carbohydrate Polymers, Elsevier, 2010, 82 (3), pp.887-894. ⟨10.1016/j.carbpol.2010.06.011⟩ |
| ISSN: | 0144-8617 |
| DOI: | 10.1016/j.carbpol.2010.06.011⟩ |
| Popis: | International audience; We have shown that hyaluronan (HA) and bovine serum albumin (BSA) are able to form electrostatic HA-BSA complexes at pH 4, whatever the length of the HA chain over the very large domain ranging from 10 3 to 10 6 g mol −1. Only the solubility of the HA-BSA complex depends on the HA chain length. The complex formation is optimum for HA chains of 50,000 g mol −1. The stoichiometry is equal to 36 HA disaccharides per BSA molecule whatever the length of the HA chain may be. This suggests that the structure of the complex greatly depends on the HA chain length: a BSA molecule surrounded by several HA fragments for small HA chain length, and an HA molecule imprisoning several BSA molecules for high HA chain length. The HA chain length can thus control accessibility of the protein surface and eventually enzyme activity. |
| Databáze: | OpenAIRE |
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