Adsorption and Conformation Behavior of Lysozyme on a Gold Surface Determined by QCM-D, MP-SPR, and FTIR.

ABSTRACT: The physicochemical properties of protein layers at the solid-liquid interface are essential in many biological processes. This study aimed to link the structural analysis of adsorbed lysozyme at the water/gold surface at pH 7.5 in a wide range of concentrations. Particular attention was paid to the protein's structural stability and the hydration of the protein layers formed at the interface. Complementary methods such as multi-parameter surface plasmon resonance (MP-SPR), quartz crystal microbalance with energy dissipation (QCM-D), and infrared spectroscopy (FTIR) were used for this purpose. The MP-SPR and QCM-D studies showed that, during the formation of a monolayer on the gold surface, the molecules' orientation changes from side-on to end-on. In addition, bilayer formation is observe

SUBMITTER: Komorek P 

PROVIDER: S-EPMC7865459 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature