Laboratory of Physical Biochemistry

savitsky2 Alexander P. Savitsky
Professor, Dr. Sci. (Chemistry)
Head of Laboratory
INBI, build. 1, room 136
Телефон +7 (495) 954-87-25 ext. 161
E-Mail  apsavitsky@inbi.ras.ru

Research directions

  • Study of caspase biochemistry in the processes of programmed cell death (apoptosis, necroptosis, autophagy)
  • Study of metalloproteinases biochemistry, regulation of its activity, search for new inhibitors in the processes of carcinogenesis, angiogenesis and inflammatory
  • Study of photophysical and photochemical properties of color fluorescent proteins from corals and its application in sub-diffraction microscopy
  • Development of sensors for the activity of caspases and metalloproteinases in living cells using genetically coded color proteins based on the principle of inductive resonance energy transfer
  • Development of methods for molecular imaging of biochemical reactions on models of small laboratory animals. Development of new methods for fluorescence tomography
  • Study of photophysical properties of dyes in the near infrared range and development of methods for its application in photodynamic therapy of tumors. Study of mechanisms and features of the immune response in photodynamic action on primary solid tumors
  • Investigation of primary photodynamic stress mechanisms in plant and animal cells
  • Investigation of mechanisms and efficiency of the population of the triplet state of chlorophyll in the photosystem of 2 chloroplasts
  • Development of methods for studying the absorption properties of molecular oxygen in biochemical systems based on direct laser excitation of oxygen molecules
  • Investigation of primary mechanisms of infrared lasers therapeutic action

Key achievements

  • Development of new classes of labels (phosphorescent and lanthanide) for immunoassay and other binding assay methods.
  • Development of methods for selective photodestruction (sterilization) of Gram-positive, Gram-negative bacteria and yeast using various porphyrins
  • Obtaining and characterizing of genetically encoded caspase 3: TR-23-K based on TagRFP monomeric protein and KFP tetramer and Tb3 + -TP-TagRFP based on terbium-binding peptide and TagRFP monomer. It showed the possibility of effective transfection and expression of the TR-23-K construct of tumor cell lines. Lentiviral transfection was chosen as the optimal method of transfection based on the rate of production of the transductant and the efficiency of its release. Three cell lines of human epidermal origin tumors transfected with the TagRFP / KFP-sensor were obtained. The proteolytic activity of caspase-3, the key enzyme apoptosis, was registered in living cells using FRET-FLIM technology and confocal microscopy. Analysis of the distribution of life time in cells allowed to discriminate apoptotic cells from living cells in the terminal cell population.
  • Creation of unique laser spectrometers for kinetic measurements of the phosphorescence of singlet oxygen in water and cell suspensions. The most accurate measurement of the lifetime of singlet oxygen in water.

Selected publications

  1. Matz M.V., Fradkov A.F., Labas Y.A., Savitsky A.P., Zaraisky A.G., Markelov M.L., Lukyanov S.A. Fluorescent proteins from nonbioluminescent Anthozoa species. – Nat Biotechnol, 1999, Oct 17(10), p. 969-73
  2. Lukyanov K.A., Fradkov A.F., Gurskaya N.G., Matz M.V., Labas Yu.A., Savitsky A.P., Markelov M.L., Zaraisky A.G., Zhao X., Fang Y., Tan W., Lukyanov S.A. Natural Animal coloration can be determined by a nonfluorescent green fluorescent protein homolog. – J.Biol.Chem., 2000, v. 275, N. 34, p. 25879-25882
  3. Alexander P. Savitsky, Alexander L. Rusanov, Victoria V. Zherdeva, Tatiana V. Gorodnicheva, Maria G. Khrenova and Alexander V. Nemukhin. FLIM-FRET Imaging of Caspase-3 Activity in Live Cells Using Pair of Red Fluorescent Proteins. -Theranostics, 2012, v. 2, N 2, pp. 215-226. (DOI:10.7150/thno.3885)
  4. B. Grigorenko, A. Savitsky, I. Topol, S. Burt, A.Nemukhin. Ground-State Structures and Vertical Excitations for the Kindling Fluorescent Protein asFP595. – J. Phys. Chem. B, 2006, v.110, p.18635-18640
  5. I.V. Turchin, V.A. Kamensky, V.I. Plehanov, A.G. Orlova, M.S. Kleshnin, I.I. Fiks, M.V. Shirmanova, I.G. Meerovich, L.R. Arslanbaeva, V.V. Jerdeva, A.P. Savitsky. Fluorescence diffuse tomography for detection of red fluorescent protein expressed tumors in small animals. – Journal of Biomedical Optics, 2008, v.13, N 4
  6. Tanja A. Schüttrigkeit, Till von Feilitzsch, Christian K. Kompa, Konstantin A. Lukyanov, Alexander P. Savitsky, Alexander A. Voityuk and Maria E. Michel-Beyerle. Femtosecond study of light-induced fluorescence increase of the dark chromoprotein asFP595. – Chemical Physics, 2006, v. 323, p. 149-160
  7. Romanova N.A., Brovko L.Y., Moore L., Pometun E., Savitsky A.P., Ugarova N.N., Griffiths M.W. Assessment of Photodynamic Destruction of Escherichia coli O157:H7 and Listeria monocytogenes by Using ATP Bioluminescence. – Applied and Environmental Microbiology, 2003, v. 69, p. 6393–6398
  8. Krasnovsky A. A. Luminescence and photochemical studies of singlet oxygen photonics. – J. Photochem. Photobiol.: A: Chem., 2008, v. 196, p. 210-218
  9. Krasnovsky A. A. Сhlorophyll isolation, structure and function: major landmarks of the early history of research in the Russian Empire and the Soviet Union. – Photosyth. Res., 2003, v. 76, p. 389-403
  10. Krasnovsky A.A., Roumbal Ya.V., Ivanov A.V., Ambartzumian R.V. Solvent depen¬den¬ce of the steady-state rate of 1O2 generation upon excitation of dissolved oxygen by cw 1267 nm laser radiation in air-saturated solutions. Estimates of the absorbance and molar absorption coefficients of oxygen at the excitation wavelength. – Chem. Phys. Lett., 2006, v. 430, p. 260-264