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EN
Lysozyme (LSZ) exhibits strong antibacterial activity against gram-positive bacteria. This property has found practical applications in the medicinal and pharmaceutical industries. Elucidating protein orientation on a nanoscale surface has important implications for integrat- ing proteins into micro- and nano-fabricated devices. Analysis of conformational changes of proteins by quartz crystal microbalance (QCM-D) and surface plasmon resonance (MP-SPR) was performed. Both methods can be used to study protein adsorption phenomena (adsorbed amount and the thickness of protein layer). A combination of QCM-D and MP-SPR methods makes it possible to draw conclusions about the factors that control the interactions between LSZ and the surface of gold. pH strongly affects the effectiveness of LSZ adsorption onto the surface and leads to orientations changes of protein on the surface. The highest adsorption value was attained near the I.E.P. This data clearly indicates that electrostatic interactions are a driving force for LSZ adsorption and significantly affect the topography of layers formed on the surface. Furthermore, these meas- urements show high hydration (60%) of LSZ layer on surface of gold.
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