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    Switchable beta-lactoglobulin (BLG) adsorption on protein resistant oligo (ethylene glycol) (OEG) self-assembled monolayers (SAMs)

    Journal: J. Colloid Interface Sci., Volume 606, JAN 15, page 1673–1683

    Authors: Skoda, Maximilian W. A.; Conzelmann, Nina F.; Fries, Madeleine R.; Reichart, Lara F.; Jacobs, Robert M. J.; Zhang, Fajun; Schreiber, Frank

    Organizations: DFG; NIST Nano-fabrication facility [N16.0028.05]

    Keywords: Protein adsorption; OEG SAMs; Protein resistance; Trivalent ions; QCM-D; Neutron reflectometry

    Hypothesis: Although protein adsorption at an interface is very common and important in biology and biotechnology, it is still not fully understood - mainly due to the intricate balance of forces that ultimately control it. In food processing (and medicine), controlling and manipulating protein adsorption, as well as avoiding protein adsorption (biofilm formation or membrane fouling) by the production of protein-resistant surfaces is of substantial interest. A major factor conferring resistance towards protein adsorption to a surface is the presence of tightly bound water molecules, as is the case in oligo ethylene glycol (OEG)-terminated self-assembled monolayers (SAMs). Due to strong attractive protein-protein and protein-surface interactions observed in systems containing trivalent salt ions, we hypothesize that these conditions may lead to a breakdown of protein resistance in OEG SAMs. Experiments: We studied the adsorption behavior of BLG in the presence of a lanthanum(III) chloride (LaCl3) at concentrations of 0, 0.1, 0.8 and 5.0 mM on normally protein resistant triethylene glycol-termianted (EG3) SAMs on a gold surface. We used quartz-crystal microbalance with dissipation (QCM-D) and neutron reflectivity (NR) to characterize the morphology of the interfacial region of the SAM. Findings: We demonstrate that the protein resistance of the EG3 SAM breaks down beyond a threshold salt concentration c* and mirrors the bulk behaviour of this system, showing reduced adsorption beyond a second critical salt concentration c**. These results demonstrate for the first time the controlled switch-ing of the protein-resistant properties of this type of SAM by the addition of trivalent salt. (c) 2021 Published by Elsevier Inc.
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