Controlling the morphological evolution of ZnO NPs from single precursor source and its application for β-lactoglobulin adsorption
Source abstract
Abstract
Control over the synthesis of morphologically different ZnO nanoparticles (NPs), using same precursor aromatic organic acid as ligand for Zn2+ co-ordination, has been reported in this study. Pyridine-2,3-dicarboxylic acid (PDC) was used as a ligand to form Zn(II)–PDC precursor complexes of different architectures, which on further calcination at 600 °C produce ZnO NPs of different morphology. The monomer Zn(II)–PDC complex leads to disk-like ZnO NPs of ~30 nm diameter, whereas the co-ordination polymer of Zn(II)–PDC when heated predominantly produce ZnO nanorod of length ~100 nm. We have also investigated the bio-interaction of these ZnO NPs with β-lactoglobulin (β-LG) adsorption study. Significantly, differential binding behavior of β-LG on these two morphologically different nanostructures has been obtained. The protein interaction process was found to be pH-dependent on disk-like ZnO NPs though thermodynamically favorable under all studied condition. The thorough analysis of the adsorption process has been performed by varying the factors such as protein and NP concentration, temperature, time, and pH. In-depth structural analysis of the protein interacting with ZnO NPs has been done using spectroscopic techniques. Fluorescence emission and anisotropy analysis reveals a partial loss in tertiary structure of β-LG upon binding on surface. However, the circular dichroism spectra show no significant change in the secondary component upon adsorption.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Polymer Surface Interaction Studies · Electrospun Nanofibers in Biomedical Applications · Proteins in Food Systems
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