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The bionanocomplexes of proteins and nanoparticles are promising bionanomaterials for medical purposes like the sensitive and the selective diagnostic devices, as well as, the modern therapeutic agents. The presence of the noble metals allows for obtaining the plasmonic effect and for generating the surface-enhanced Raman scattering phenomenon (SERS). The knowledge of the nanoparticle interaction with the protein molecule is extremely necessary for the development of the suitable product. The interaction of the bionanocomplex components can cause the conformational changes in the protein structure and the modification of surface properties of the nanoparticles. In the case of the binding of the gold nanoparticles with the enzymes, it is critical to preserve the catalytic activity, which is connected with maintaining the proper molecule structure. In the presented study, the Fourier transform infrared spectroscopy was used for the investigation of the interaction and the structural properties of the cholesterol oxidase (ChOX)—the gold nanoparticles bionanocomplex. The ChOX is one of the most important enzymes for the medical diagnostics and the promising antibacterial agent. The infrared spectra of the AuNP-ChOX bionanocomplex and the ChOX in different forms (the solid and the suspended in the buffer) are presented and discussed. The obtained spectra include the considerable number of the absorption lines identified and attributed to the corresponding chemical bonds and the functional groups of the protein. The analysis of the obtained infrared spectra revealed the important information about the changes of the protein structure after the immobilization on the gold nanoparticles. Moreover, it allows to recognize the differences in the structure of the protein in a different environment, which is of great importance in the context of bionanotechnology.

journal of nanoparticle research

Interaction of gold nanoparticles with cholesterol oxidase enzyme in bionanocomplex—determination of the protein structure by Fourier transform infrared spectroscopy