Lida Momeni Borujeni
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 ...
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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.
Lida Momeni; Sadegh Farhadian; Behzad Shareghi
Volume 4, Issue 4 , May 2016, , Pages 1-9
Abstract
Abstract Adsorption of proteins on inorganic surfaces may lead to structural and functional changes that are dependent on both the nature of the adsorbed proteins and the physicochemical properties of the inorganic surfaces. Chicken egg white lysozyme (E.C 3.2.1.17, MW=14.6 kDa) is a small globular protein, ...
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Abstract Adsorption of proteins on inorganic surfaces may lead to structural and functional changes that are dependent on both the nature of the adsorbed proteins and the physicochemical properties of the inorganic surfaces. Chicken egg white lysozyme (E.C 3.2.1.17, MW=14.6 kDa) is a small globular protein, that consists of 129 amino acid residues with four disulfide bonds. The aim of this study was the survey of the stability and structure of Chicken egg white lysozyme against ZnO nano through thermal stability, fluorescence and spectroscopy and enzyme activity assay in the absence or presence of ZnO nano particle at pH 7.0. The obtained results indicated that thermal stability and activity of lysozyme decreased with increase in ZnO nanoparticles concentration. Moreover, it was observed that ZnO Nano particle quenched the intrinsic fluorescence of lysozyme. The interaction studies of ZnO nanoparticles and lysozyme show that not only water and solvent molecules can effect on 3D structure of lysozyme and protein but also play an important role in adsorption nanoparticles.
