In this work, we present a sensitive method for the determination of the enzyme concentration of cholesterol oxidase, which is one of the most important analytical enzymes. Although the method is affected by sensitivity limitations, recently the Raman scattering experimental data carried out on cholesterol oxidase conjugated via a 16-mercaptohexadecanoic acid organic linker with gold nanoparticles due to the surface plasmon resonance confirmed the observation of surface enhanced Raman scattering, which enables us to detect the vibrational lines belonging to PO and C=C bonds assigned to the flavin prosthetic group. This means there is a stable binding of the enzyme with nanoparticles as well as the enzyme remaining active and substantiates the possibility that prepared bio-nanosystems can be used for analytical purposes as a sensing element.
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 surfaceenhanced 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.
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