Laboratory of Peptide chemistry

Department of Peptide and Protein Technologies

Head: Vadim Ivanov, member of the academy of sciences
ivavt@ibch.ru+7(495)330-56-92

NamePositionContacts
Vadim Ivanov, member of the academy of sciencesdepart. dir.ivavt@ibch.ru+7(495)330-56-92
Vladimir Demushkin, D.Scl. r. f.vpdem@ibch.ru+7(495)330-64-38
Andrej Karelin, D.Scl. r. f.+7(495)3353200#4002
Inessa Mikhaleva, Ph.D.l. r. f.inessamikh@rambler.ru+7(495)3355366
Alexandr Skripnikov, Ph.D.s. r. f.a.skripnikov@gmail.com
Evgenij Efremov, Ph.D.s. r. f.+7(495)330-64-38
Ljudmila Alekseeva, Ph.D.r. f.Luda.alekseeva@mail.ru+7(495)335-61-77
Tat'jana Gogitidzer. f.+7(495)330-74-92
Svetlana Guryanova, Ph.D.r. f.svgur@mail.ru+7(495)335-61-77
Vladislav Dejgin, D.Scr. f.vdeigin@gmail.com+7(495)330-72-38
Elena Mewerjakova, Ph.D.r. f.eam@ibch.ru+7(495)3356177
Ljudmila Onoprienko, Ph.D.r. f.onolv@mail.ru+7(495)3361300
Igor' Prudchenko, Ph.D.r. f.iaprud@ibch.ru+7(495)3355366
Marina Filippova, Ph.D.r. f.
Dar'ja Dement'eva, Ph.D.r. f.dariad@mx.ibch.ru+7(495)330-40-11
Natal'ja Egorovaj. r. f.+7(495)335-58-44
Olga Ksenofontova, Ph.D.j. r. f.
Elena Tolchevaj. r. f.+7(495)335-23-11
Dmitry Khachinj. r. f.Khachin@ibch.ru
Alisa Lyazninaj. r. f._alice_55@mail.ru
Alexandra ShevchenkoPhD stud.ashevchenko87@mail.ru
Svetlana Volkovat. q. - lab. as.+7(495)335-32-00
Evgeniya Lukachevat. q. - lab. as.euhenita@ya.ru
Elena Dobrushkinares. eng.+7(495)335-61-77
Elena Zhavoronkovares. eng.+7(495)330-74-92
Evgenij Makarovres. eng.+7()3356177
Zhanna Trifonova, Ph.D.res. eng.

Former members:

Tat'jana Andronova, Ph.D.s. r. f.tmap@mail.ru

Selected publications

  1. Яцкин О.Н., Карелин А.А., Иванов В.Т. (2009). Пептидомы мозга, сердца, легких и селезенки крысы: сходство и различия. Биоорг. хим. 35 (4), 471–482 ID:233
  2. Stoilova T.B., Kovalchuk S.I., Egorova N.S., Surovoy A.Y., Ivanov V.T. (2008). Gramicidin A-based peptide vector for intracellular protein delivery. Biochim. Biophys. Acta 1778 (10), 2026–31 [+]

    The development of the peptide-based vectors for the intracellular delivery of biologically active macromolecules has opened new prospects of their application in research and therapy. Earlier the amphipathic cell-penetrating peptide (CPP) Pep-1 was reported to mediate cellular uptake of proteins without covalent binding to them. In this work we studied the ability of a series of membrane-active amphipathic peptides, based on the gramicidin A sequence, to transport a model protein across the eukaryotic cell membrane. Among them the positively charged Cys-containing peptide P10C demonstrated the most effective beta-galactosidase intracellular delivery. Besides, this peptide was shown to form noncovalent associates with beta-galactosidase as judged from electrophoresis and enzymatic activity assays. In addition, a series of new gramicidin analogues were prepared and the effect of N-terminus modification of gramicidin on the protein transduction efficiency was studied.

    ID:232
  3. Тепкеева И.И., Моисеева Е.В., Чаадаева А.В., Жаворонкова Е.В., Кесслер Ю.В., Семушкина С.Г., Дёмушкин В.П. (2008). Оценка противоопухолевой активности пептидных экстрактов растений в перевиваемой модели рака молочной железы на мышах линии CBRB-Rb(8.17)1lem. Бюл. эксперим. биологии и медицины 145 (4), 446–448 ID:243
  4. Михалева И.И., Рихирева Г.Т., Прудченко И.А., Голубев И.Н. (2006). Взаимодействие дельта-сон индуцирующего пептида и его аналогов с клеточными мембранами и структурно- функциональный анализ. Биоорг. хим. 32 (2), 176–182 ID:229
  5. Ivanov V.T., Yatskin O.N. (2005). Peptidomics: a logical sequel to proteomics. Expert review of proteomics 2 (4), 463–73 [+]

    Rapid progress of separation techniques as well as methods of structural analysis provided conditions in the past decade for total screening of complex biologic mixtures for any given class of biomolecules. The present review updates the reader with the modern state of peptidomics, a chapter of chemical biology that deals with structure and biologic properties of sets of peptides present in biologic tissues, cells or fluids. Scope and limitations of currently employed experimental techniques are considered and the main results are outlined. Considerable attention will be afforded to the biologic role of peptides formed in vivo by proteolysis of nonspecialized precursor proteins with other well-defined functions. In conclusion, the connection is discussed between peptidomics and the much more mature and still closely related field of proteomics.

    ID:226
  6. Ivanov V.T., Karelin A.A., Yatskin O.N. (2005). Generation of peptides by human erythrocytes: facts and artifacts. Biopolymers 80 (2-3), 332–46 [+]

    Previously reported data on peptide composition of human erythrocyte lysate were obtained under conditions that did not exclude proteolytic degradation of hemoglobin in the process of peptide isolation. Comparative chromatographic analysis of the diluted erythrocyte lysate incubated in acidic conditions with or without proteolytic enzyme inhibitors showed that several peptides earlier identified as intraerythrocyte ones in fact result from hemoglobin degradation by erythrocyte acidic protease(s) during incubation of the lysate. A rational scheme excluding postlysis proteolysis was developed for isolation of peptide fraction. Further analysis resulted in determination of structure and content of about 50 endogenous intraerythrocyte hemoglobin fragments. A primary endopeptidase splitting of alpha- and beta-globin chains followed by consecutive exopeptidase trimming of primary fragments is suggested as a degradation mechanism. The intraerythrocyte peptides were shown to differ from peptides excreted by the erythrocytes to the extracellular medium in the primary culture. It was also found that intraerythrocyte peptides cannot play the role of precursors of hemoglobin fragments present in tissue extracts.

    ID:227
  7. Blishchenko E.Y., Sazonova O.V., Kalinina O.A., Moiseeva E.V., Vass A.A., Karelin A.A., Ivanov V.T. (2005). Antitumor effect of valorphin in vitro and in vivo: combined action with cytostatic drugs. Cancer Biol. Ther. 4 (1), 118–24 [+]

    The action of the cytostatic drugs (epirubicin and vincristine) in combination with the endogenous antiproliferative beta-hemoglobin fragment (33-39), valorphin, was studied in tumor (L929 and A549) cell cultures, primary culture of murine bone marrow cells and in murine model of breast carcinoma in vivo. Simultaneous application of 1 microM valorphin and 1 microM epirubicin, in vitro, did not result in an additive suppressive effect on cell culture growth. Additive effects were achieved with alternating applications of the peptide and the drugs, namely, 0.5 microM (but not 1 microM) epirubicin added 24 h prior to 1 microM valorphin; 1 microM valorphin added 48 h prior to 0.1 microM epirubicin, or 0.1 microM vincristine, or 0.05 microM vincristine, which resulted in 100% cell death in the both series with vincristine and up to 78% cell biomass reduction in the experiments with epirubicin. In the in vivo model (female BLRB mice with subcutaneously inoculated syngeneic mammary carcinoma), simultaneous treatment with 25 mg/m(2) epirubicin and 1 mg/kg valorphin resulted in 42% of tumor growth inhibition, as compared with the negative control group and 22% inhibition as compared with the epirubcin-treated group (at 20th day of treatment). Survival was significantly improved (69% compared to 39% in the group treated with epirubicin only) at day 26 after the treatment beginning.

    ID:228
  8. Ovchinnikov Y.A., Ivanov V.T., Evstratov A.V., Sumskaya L.V., Melnik E.I., Chumburidze T.S., Portnova S.L., Balashova T.A. (1973). Sandwich complexes as a functional form of the enniatin ionophores. FEBS Lett. 36 (1), 65–71 [+]

    The ability of the enniatin cyclodepsipeptides (CDP) (fig. 1) to form complexes with alkali metal ions (M+) and induce ionic permeability in artificial and biological membranes has been described in a number of papers [ 1,2]. The complexes were found to be equimolar in both solutions and in the crystalline state; by analogy with valinomycin and the nactins the role of the M+ carriers across the membrane was ascribed to them [3,49. In the present paper evidence is produced showing that an important part in the functioning of this group of ionophores is played by complexes with 2: 1 and 3:2 macrocycle:cation ratios.
     

    ID:141
  9. Ovchinnikov Yu.A., Shemyakin M.M., Ivanov V.T., Antonov V.K., Vinogradova E.I., Shkrob A.M., Malenkov G.G., Evstratov A.V., Laine I.A., Melnik E.I., Ryabova I.D. (1969). Cyclodepsipeptides as chemical tool for studying ionic transport through membranes. J. Membr. Biol. 1, 402–403 [+]

    This paper reports a study of the chemistry of valinomycin, enniatins and related membrane-active depsipeptides that increase alkali metal ion permeability of model and biological membranes. The antimicrobial activity of these compounds and thir effect on membranes has been correlated with their cation-complexing ability. the complexing reaction has been studied by spectropolarimetric studies have revealed coexistence of conformers of the cyclopeptides and conductometric methods.  Nuclear magnetic resonance, optical rotatory dispersion, and infrared spectrophotometric studies have revealed the coexistence ofconformers of the cyclodepsipeptides in solution and have led to elucidation of the spatial structure of valinomycin, enniatin B and their K+ complexes. The effect of the conformational properties of the cyclodepsipeptides on their complexation efficiency and selectivity, surface-active properties and behavior towards phospholipid monolayers, bimolecular phospholipid membranes and a number of biological membrane systems has been ascertained. The studies have clearly shown the feasibility of using cyclodepsipeptides with predetermined structural and conformational parameters as chemical tools for membrane studies. It is suggested that the principle of conformation-dependent cation binding through ion-dipole interactions may possibly lie at the basis of the mode of action of systems governing the natural ion permeability in biological membranes.

    ID:142
  10. Ovchinnikov Yu.A., Shemyakin M.M., Kiryushkin A.A., Kozhevnikova I.V. (1965). Synthesis of peptides in solution on polymeric support: 1. Synthesis of glycylglycyl-L-leucylglycine. Tetrahedron Lett. 27, 2323–2327 ID:138

Vadim Ivanov

  • Russia, Moscow, Ul. Miklukho-Maklaya 16/10 — On the map
  • IBCh RAS, build. 51, office. 454
  • Phone: +7(495)330-56-92
  • E-mail: ivavt@ibch.ru