Adsorption and conformation behavior of lysozyme on a gold surface determined by qcm‐d, mp‐spr, and ftir

Komorek, Paulina and Martin, Elisha and Jachimska, Barbara (2021) Adsorption and conformation behavior of lysozyme on a gold surface determined by qcm‐d, mp‐spr, and ftir. International Journal of Molecular Sciences, 22 (3). 1322. ISSN 1661-6596 (

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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 mono-layer on the gold surface, the molecules' orientation changes from side‐on to end‐on. In addition, bilayer formation is observed when adsorbing in the high‐volume concentration range >500 ppm. The degree of hydration of the monolayer and bilayer varies depending on the degree of surface coverage. The hydration of the system decreases with filling the layer in both the monolayer and the bilayer. Hydration for the monolayer varies in the range of 50‐70%, because the bilayer is much higher than 80%. The degree of hydration of the adsorption layer has a crucial influence on the protein layers' viscoelastic properties. In general, an increase in the filling of a layer is characterized by a rise in its rigidity. The use of infrared spectroscopy allowed us to determine the changes taking place in the secondary structure of lysozyme due to its interaction with the gold surface. Upon ad-sorption, the content of II‐structures corresponding to β‐turn and random lysozyme structures in-creases, with a simultaneous decrease in the content of the β‐sheet. The increase in the range of β‐ turn in the structure determines the lysozyme structure's stability and prevents its aggregation.