Adsorption of Milk Proteins (β-Casein and β-Lactoglobulin) and BSA onto Hydrophobic Surfaces
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ProteinsQCMMD simulationsHydrophobic effectIon condensationElectrokinetic mobility
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]
PatrocinadorThe authors wish to thank the financial support granted by the project CTS-6270 (Junta de Andalucía, Spain) and the Spanish “Ministerio de Economía y Competitividad (MINECO), Plan Nacional de Investigación, Desarrollo e Innovación Tecnológica (I + D + i)” (Project FIS2016-80087-C2-1-P). J.F.acknowledges financial support from the Spanish Ministry of Economy and Competitiveness, through the “Severo Ochoa” Programme for Centres of Excellence in R & D (SEV-2015-0496) awarded to ICMAB. L.P.-F. thanks the financial support provided by the COST Action MP1303: Understanding and Controlling Nano and Mesoscale Friction.
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.