Abstract
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.
Highlights
Cardiovascular diseases are the most common causes of disability and mortality (32% of the deaths in the Global Burden of the Disease Study report)
The risk related to the burden of the disease and the health effects is associated with many risk factors, among which, the high cholesterol level is estimated as the most significant, causing numerous deaths (Global Burden of Disease Collaborative Network 2016)
The Fourier transform infrared spectroscopy (FTIR) was used as the versatile tool to study the protein conformation of the cholesterol oxidase (ChOX) enzyme immobilized on the surface of AuNP via linker
Summary
Cardiovascular diseases are the most common causes of disability and mortality (32% of the deaths in the Global Burden of the Disease Study report). The extensive researches on constructing the modern electrochemical as well as the optical biosensors for the cholesterol are carried out For this purpose, the bionanocomplexes of the ChOX and the noble metal nanoparticles (MNPs) are prepared. The Fourier transform infrared spectroscopy (FTIR) was used as the versatile tool to study the protein conformation (including the secondary structure) of the ChOX enzyme immobilized on the surface of AuNP via linker. This method is suitable for the biological materials, including the proteins and the enzymes (Baker et al 2014) It provides an important information about the structure of the molecules, their interactions, the mechanisms of protein reactions, and the conformational changes (Barth 2007; Dembereldorja et al 2012). The prepared bionanocomplex was washed and suspended in the phosphate buffer (the 50 mM, pH 7.5) to obtain the 0.5 mg/ml concentration of the ChOX enzyme. The obtained information was taken into an account to fit the band by the Lorenzian and Gaussian functions
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