The Displacement of Preadsorbed Protein with a Cationic Surfactant at the Hydrophilic SiO2−Water Interface

Autor:	Jian R. Lu, and T. J. Su, Rebecca J. Green, J. R. P. Webster
Rok vydání:	2001
Předmět:	Range (particle radiation) Hydrogen Chemistry Inorganic chemistry Cationic polymerization chemistry.chemical_element Surfaces Coatings and Films chemistry.chemical_compound Adsorption Deuterium Pulmonary surfactant Materials Chemistry Physical and Theoretical Chemistry Lysozyme Layer (electronics)
Zdroj:	The Journal of Physical Chemistry B. 105:9331-9338
ISSN:	1520-5207 1520-6106
DOI:	10.1021/jp0106247
Popis:	Neutron reflectivity has been used to investigate the interaction between the cationic surfactant dodecyltrimethylammonium bromide (C12TAB) and preadsorbed lysozyme layers at the hydrophilic silica−water interface. Reflectivity measurements were carried out with two different concentrations of lysozyme and a range of C12TAB concentrations at a solution pH of 7. A preadsorbed lysozyme layer was prepared by adsorption from 0.03 or 1 g dm-3 protein solutions. The effect on the adsorbed protein layer structure upon addition of a range of surfactant concentrations, from 0.2 to 14 mM, was determined and the surface excesses of both protein and surfactant within the adsorbed layers calculated. The surface composition of the mixed layers and their structural distributions were identified with the help of the variation of hydrogen/deuterium labeling to the surfactant. It was found that upon increasing surfactant concentration the protein was gradually replaced by the surfactant at the interface. However, a simple ...
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::b59649131aed07beb4460768bbaa6b4f https://doi.org/10.1021/jp0106247 Zobrazit plný text záznamu