In situ studies of bovine serum albumin adsorption onto functionalized polystyrene latices monitored with a quartz crystal microbalance technique |
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Authors: | Manel Beragoui Chadlia Aguir Mohamed Khalfaoui Eduardo Enciso Maria José Torralvo Laurent Duclaux Laurence Reinert Marylène Vayer Abdelmottaleb Ben Lamine |
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Affiliation: | 1. Unité de Recherche de Physique Quantique, Faculté des Sciences de Monastir, Université de Monastir, Monastir, Tunisia;2. Unité de Recherche de Chimie Appliquée et Environnement, Faculté des Sciences de Monastir, Université de Monastir, Monastir, Tunisia;3. Departamento de Química Física I, Facultad de Ciencias Químicas, Universidad Complutense, Spain;4. Laboratoire de Chimie Moléculaire et Environnement, Université, de Savoie, France;5. Centre de Recherche sur la Matière Divisée, 1b Rue de la Férollerie, Orléans, France |
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Abstract: | The adsorbability of bovine serum albumin (BSA) onto poly(styrene‐co‐itaconic acid) (PS–IA), poly(styrene‐co‐hydroxyethyl methacrylate) (PS–HEMA), poly(styrene‐co‐acrylic acid) (PS–AA), and poly(styrene‐co‐methacrylic acid) (PS–MAA) latices were investigated with a quartz crystal microbalance. The amount adsorbed onto the functionalized latices, except for PS–MAA, was greater than that adsorbed onto polystyrene (PS) latex. To explain this result, two kinds of interaction forces were considered, hydrogen bonding and hydrophobic interactions, whereas electrostatic interaction was assumed to be small. When comparing the two extremes of hydrophobic interaction and hydrogen bonding, the latter was stronger. The corrected adsorption mass suggested that the BSA molecules were adsorbed onto the PS–MAA latex in a side‐on mode. However, in the case of the PS, PS–IA, PS–HEMA, and PS–AA latices, the BSA molecules were probably adsorbed in multiple layers. The presence of the BSA in the latex particle surface was verified by attenuated total reflectance/Fourier transform infrared spectroscopy and atomic force microscopy. © 2015 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2015 , 132, 42055. |
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Keywords: | adsorption copolymers proteins surfaces and interfaces |
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