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In-Line Characterization of the Temperature-Responsive Behavior of Surface-Bound Microgel Coatings by QCM-D: A Novel Strategy for Protein Repellence Evaluation.

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In this work, quartz crystal microbalance with dissipation monitoring (QCM-D) was used to develop a new method to evaluate the protein repellency of microgel coatings. Compared to traditional protocols for… Click to show full abstract

In this work, quartz crystal microbalance with dissipation monitoring (QCM-D) was used to develop a new method to evaluate the protein repellency of microgel coatings. Compared to traditional protocols for surface analysis, QCM has the advantage of a real-time quantitative approach with high sensitivity, allowing us to describe variations of the adsorbed mass with unprecedented accuracy. To enable the detectability of the film throughout the whole operational temperature interval, a poly(N-isopropylacrylamide-co-glycidyl methacrylate) p(NIPAm-co-GMA) microgel monolayer with defined thickness and rigidity was designed. Covalent adhesion of the film to the silica surface was achieved by epoxy-thiol click chemistry and tested for repeated temperature cycles, showing substantial reproducibility. Further functionalization of microgel surfaces by grafting polyzwitterionic chains remarkably improved the protein repellence leaving the strong surface adhesion unaltered. Before and after exposure to fluorescein-tagged bovine serum albumin (FITC-BSA), the coatings showed identical responsive behavior, proving the absence of protein deposition. In nonrepellent coatings, QCM monitoring instead displayed a characteristic shift in the volume phase transition (VPT), pointing out the effect of adsorbed proteins on the swelling behavior of pNIPAm. The combination of QCM-D and UV-visible (UV-vis) was used to evaluate the effect of increasing surface coverage, enabling to distinguish between the protein deposition occurring over the coated and the uncoated portion of the sensor.

Keywords: protein repellence; responsive behavior; microgel coatings; surface; temperature; protein

Journal Title: ACS applied materials & interfaces
Year Published: 2022

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