Abstract
The bioactivity features of shungite nanocarbon (ShC) as a new ultrafine carbon form are of particular interest from the point of view of both biomedical applications of the nanomaterial and environmental issues. Thermodynamic effects of human serum albumin (SA) interaction with ShC in water nanodispersion have been studied regarding the molecular structure and protein fraction content using differential scanning calorimetry. Deconvolution of the albumin denaturation curve on the basis of Gaussian functions was used to analyze the characteristics (temperature, enthalpy) of individual endothermic transitions of the protein. The increase of the temperature difference of individual transitions was found to be the major SA-ShC interaction effect. No overall thermal destabilization of the protein was observed, although some partial destabilization did occur. This result cannot ensue from changes in intramolecular interdomain interactions in protein molecules at intermolecular interactions with ShC since only a small part of the total protein in nanodispersion has access to nanoparticle surface. The effects observed are shown to be related to the ShC influence on the ratio of the protein fractions with different fatty acids (FA) content by affecting some part of FA at their protein binding sites and their transition to nanoparticles. Protein and nanocarbon probably compete for FA in the process, and their concentration ratio in the dispersion is of decisive importance. The significance of this sort of competition consists in the possibility to influence the transport function of serum albumin with respect to FA.
Highlights
The bioactivity features of shungite nanocarbon (ShC) as a new ultrafine carbon form are of particular interest from the point of view of both biomedical applications of the nanomaterial and environmental issues
No overall thermal destabilization of the protein was observed, some partial destabilization did occur. This result cannot ensue from changes in intramolecular interdomain interactions in protein molecules at intermolecular interactions with ShC since only a small part of the total protein in nanodispersion has access to nanoparticle surface
The effects observed are shown to be related to the ShC influence on the ratio of the protein fractions with different fatty acids (FA) content by affecting some part of FA at their protein binding sites and their transition to nanoparticles
Summary
Особенности механизма биоактивности шунгитового наноуглерода (ShC), как новой ультрадисперсной формы углерода, представляют большой интерес с точки зрения биомедицинских приложений наноматериала и охраны окружающей среды. Термодинамические эффекты взаимодействия ShC с сывороточным альбумином (СА) человека в водной нанодисперсии исследовались методом дифференциальной сканирующей калориметрии в аспекте молекулярной структуры и фракционного состава белка. Protein and nanocarbon probably compete for FA in the process, and their concentration ratio in the dispersion is of decisive importance The significance of this sort of competition consists in the possibility to influence the transport function of serum albumin with respect to FA. Понимание фундаментальных взаимодействий новых ультрадисперсных форм углерода с биологическими молекулами, тканевыми структурами и целыми организмами является первоочередным с точки зрения как биомедицинских приложений, так и охраны окружающей среды [Wang et al, 2016]. За счет взаимодействия с наночастицами углерода также может быть повышен потенциал СА как носителя органических лигандов
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