Publication | Closed Access
Laser-optical investigation of the effect of diamond nanoparticles on the structure and functional properties of proteins
31
Citations
6
References
2011
Year
Optical MaterialsFunctional PropertiesEngineeringColloidal NanocrystalsFtir SpectrumProtein NanoparticlesOptical PropertiesBioanalysisBioimagingLaser-optical InvestigationBiophysicsBiochemistryInfrared SpectroscopyDiamond NanoparticlesBiophotonicsBiomolecular ScienceBiomolecular EngineeringDiamond-like CarbonLaser PhotochemistryBiomedical DiagnosticsNatural SciencesSpectroscopyBiomolecular SpectroscopyOptical TrappingMolecular BiophysicsProtein AdsorptionSpectroscopic Method
Adsorption of such blood plasma proteins as albumin and g-globulin on diamond nanoparticles of size around 5 nm and around 100 nm is observed and studied using laser-optical methods. The adsorption of blood plasma proteins at physiological pH 7.4 is found weaker than that of enzyme protein lysozyme. The observed variations in the Fourier Transform Infrared (FTIR) spectra of proteins may be due to structural transformations of the adsorbed protein. Using the lysozyme as a test protein we show that the protein adsorption leading to observable changes in the FTIR spectrum (the band of Amide I) also induces a significant decrease in the protein functional activity. It is also found that the influence of ∼5-nm diamond nanoparticles on the protein structure and functions is more significant than that of ∼100-nm nanodiamonds.
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