Abstract

Polymer brushes of different structure (full extension vs collapsed) and charge (+, 0 −) have been employed as supporting “smart” interface for investigating the recrystallization pathways of isolated SbpA bacterial surface proteins. Such study has been done by means of Quartz Crystal Microbalance with Dissipation monitoring (QCMD), which allowed following the real-time evolution of frequency (related to the adsorbed mass per area) and dissipation (elastic properties) factors, either individually or combined as the so-called Df plots. Results showed higher affinity of SbpA for positively charged brushes with poly{[2-(methacryloyloxy)ethyl] trimethylammonium chloride} (PMETAC) in their composition as well as for negative poly(sulfo propyl methacrylate) (PSPM) brushes which were grown in limited chain extension conditions. The crystal structure of the formed layer could be elucidated by complementary Atomic Force Microscopy (AFM).

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