Journal
QUANTUM ELECTRONICS
Volume 40, Issue 12, Pages 1089-1093Publisher
TURPION LTD
DOI: 10.1070/QE2010v040n12ABEH014507
Keywords
laser-optical methods; FTIR spectroscopy; nanodiamond; blood plasma proteins; adsorption
Funding
- Russian Foundation for Basic Research [08-02-92002]
- NSC of Taiwan [NSC 97-2923-M-259-001-MY3]
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Adsorption of such blood plasma proteins as albumin and gamma-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 similar to 5-nm diamond nanoparticles on the protein structure and functions is more significant than that of similar to 100-nm nanodiamonds.
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