Adsorption of Milk Proteins (β-Casein and β-Lactoglobulin) and BSA onto Hydrophobic Surfaces Pérez Fuentes, Leonor Drummond, Carlos Faraudo Gener, Jordi Bastos González, Delfina María Proteins QCM MD simulations Hydrophobic effect Ion condensation Electrokinetic mobility Here, we study films of proteins over planar surfaces and protein-coated microspheres obtained from the adsorption of three different proteins ( β -casein, β -lactoglobulin and bovine serum albumin (BSA)). The investigation of protein films in planar surfaces is performed by combining quartz crystal microbalance (QCM) and atomic force microscopy (AFM) measurements with all-atomic molecular dynamics (MD) simulations. We found that BSA and β -lactoglobulin form compact monolayers, almost without interstices between the proteins. However, β -casein adsorbs forming multilayers. The study of the electrokinetic mobility of protein-coated latex microspheres shows substantial condensation of ions from the buffer over the complexes, as predicted from ion condensation theories. The electrokinetic behavior of the latex-protein complexes is dominated by the charge of the proteins and the phenomenon of ion condensation, whereas the charge of the latex colloids plays only a minor role. 2017-09-27T10:54:10Z 2017-09-27T10:54:10Z 2017-08-02 info:eu-repo/semantics/article Pérez Fuentes, L.; et al. Adsorption of Milk Proteins (β-Casein and β-Lactoglobulin) and BSA onto Hydrophobic Surfaces. Materials, 10(8): 893 (2017). [http://hdl.handle.net/10481/47559] 1996-1944 http://hdl.handle.net/10481/47559 10.3390/ma10080893 eng info:eu-repo/semantics/openAccess MDPI