A. M. Saletskii

Publications (3)1.64 Total impact

• Article: Triplet-triplet energy transfer between luminescent probes bound to albumins

  A. G. Mel’nikov, A. M. Saletskii, V. I. Kochubey, A. B. Pravdin, I. S. Kurchatov, G. V. Mel’nikov
  [show abstract] [hide abstract]
  ABSTRACT: The interaction of polar and nonpolar luminescent probes with human blood serum albumins is studied by absorption and luminescence spectroscopy. It is found that the probes (polar eosin and nonpolar anthracene) can efficiently bind to proteins. The radii of the quenching spheres of energy-donor (eosin) triplet states in the presence of an acceptor (anthracene) in the process of the triplet-triplet energy transfer in proteins are determined for homogeneous and inhomogeneous distributions of acceptor molecules over the solution volume. It is shown that a decrease in the radius of the quenching sphere observed upon the addition of sodium dodecylsulfate surfactant is caused by structural changes in the protein.
  Optics and Spectroscopy 04/2012; 109(2):188-192. · 0.61 Impact Factor
• Article: Complexation of pyrene and anthracene with human blood plasma

  A. M. Saletskii, A. G. Mel’nikov, A. B. Pravdin, V. I. Kochubei, G. V. Meln’ikov
  [show abstract] [hide abstract]
  ABSTRACT: We have studied the interaction between polycyclic aromatic hydrocarbons (pyrene and anthracene) with human serum albumin (HSA) and human blood plasma. We have shown that the increase in the fluorescence intensity and the decrease in the polarity index of pyrene on going from an aqueous solution to a pH 7.4 buffer solution of HSA suggests that polycyclic aromatic hydrocarbons are localized in the hydrophobic microphase of the proteins. The increase in the fluorescence intensity for anthracene and pyrene, and also the decrease in the polarity index of pyrene on going from HSA to blood plasma is connected with the fact that polycyclic aromatic hydrocarbons can bind both to plasma proteins and to plasma lipids. When sodium dodecyl sulfate (SDS) is added to the blood plasma in a concentration greater than the critical micelle concentration, we observe an increase in the fluorescence intensity and the polarity index of pyrene. We hypothesize that this is connected with localization of pyrene near the interface between the hydrophobic and hydrophilic phases of the protein-SDS system. We have established that SDS leads to a change in the structure of blood plasma proteins and promotes escape of polycyclic aromatic hydrocarbons from the protein globules.
  Journal of Applied Spectroscopy 04/2008; 75(3):402-406. · 0.51 Impact Factor
• Article: Structural Changes in Human Serum Albumin According to the Data on the Phosphorescence Kinetics of a Luminescent Probe — Eosin

  A. M. Saletskii, A. G. Mel'nikov, A. B. Pravdin, V. I. Kochubei, G. V. Mel'nikov
  [show abstract] [hide abstract]
  ABSTRACT: The influence of the human serum albumin (HSA) denaturation by a surface-active substance (sodium dodecyl sulfate (SDS)) on the phosphorescence of a luminescent probe (eosin) has been investigated. The dependences of the eosin-phosphorescence intensity on the SDS concentration were determined at different pH levels of an HSA solution. It has been shown that at SDS concentrations lower than the critical concentration necessary for micelle formation, the hydrophobic interactions of eosin with the protein influence the deactivation of the eosin triplet states.
  Journal of Applied Spectroscopy 08/2005; 72(5):723-727. · 0.51 Impact Factor