Document Type : Article
Author
Assistant Professor of Biology, Department of Science, Payame Noor Niversity, Iran.
Abstract
In this study, the effect of iron oxide nanoparticles on the structure, thermal stability and activity of bovine pancreatic trypsin was investigated. Various spectroscopic techniques including UV absorption, circular distortion, thermal stability, fluorescence and kinetics at pH 8 were used to achieve this goal. Thermodynamic and kinetic results showed that trypsin stability decreased in the presence of iron oxide nanoparticles and increased its activity. Fluorescence spectroscopy showed that the nanoparticles can reduce trypsin fluorescence through static quenching. Based on the thermodynamic parameters, the process of binding the nanoparticles to trypsin is performed as a spontaneous reaction which the electrostatic forces play the main role in. Circular dichroism studies showed changes in the secondary structure of trypsin as an increase in α-Helix l content and a decrease in β-sheets. UV spectroscopy showed that iron oxide nanoparticles bind to trypsin and cause changes in protein structure. The interaction studies of Fe3O4 nanoparticles and trypsin show that not only water and solvent molecules can affect on 3D structure of trypsin and protein but also play an important role in adsorption nanoparticles.
Keywords
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