Adsorption and conformation behavior of lysozyme on a gold surface determined by qcm‐d, mp‐spr, and ftir
| العنوان: | Adsorption and conformation behavior of lysozyme on a gold surface determined by qcm‐d, mp‐spr, and ftir |
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| المؤلفون: | Elisha Martin, Paulina Komorek, Barbara Jachimska |
| المصدر: | International Journal of Molecular Sciences, Vol 22, Iss 1322, p 1322 (2021) International Journal of Molecular Sciences Volume 22 Issue 3 |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | conformation, 02 engineering and technology, 01 natural sciences, Protein Structure, Secondary, lcsh:Chemistry, chemistry.chemical_compound, Spectroscopy, Fourier Transform Infrared, lysozyme adsorption, QD, Surface plasmon resonance, lcsh:QH301-705.5, Spectroscopy, Bilayer, viscoelastic properties, gold surface, General Medicine, Hydrogen-Ion Concentration, 021001 nanoscience & nanotechnology, Computer Science Applications, Lysozyme, 0210 nano-technology, hydration, Materials science, Surface Properties, Infrared spectroscopy, QCM-D, 010402 general chemistry, MP-SPR, Article, Catalysis, Inorganic Chemistry, Adsorption, Monolayer, Physical and Theoretical Chemistry, Fourier transform infrared spectroscopy, Molecular Biology, Organic Chemistry, Water, Quartz crystal microbalance, Surface Plasmon Resonance, 0104 chemical sciences, FTIR, lcsh:Biology (General), lcsh:QD1-999, Chemical engineering, chemistry, Quartz Crystal Microbalance Techniques, Muramidase, Gold |
| الوصف: | 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 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 adsorption, the content of II-structures corresponding to β-turn and random lysozyme structures increases, 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. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 1661-6596 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bf3a7e82f1625d346ec0abe781150da https://strathprints.strath.ac.uk/75517/1/Komorek_etal_IJMS2021_Adsorption_conformation_behavior_lysozyme_gold_surface.pdf |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....8bf3a7e82f1625d346ec0abe781150da |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16616596 |
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