PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
Tytuł artykułu

Peptydoglikan : budowa, rola biologiczna oraz synteza

Treść / Zawartość
Identyfikatory
Warianty tytułu
EN
Peptidoglycan : structure, biological activity and chemical synthesis
Języki publikacji
PL
Abstrakty
EN
The most important component of bacterial cell walls especially Gram-positive bacteria is peptidoglycan, called also murein, PGN. The first time this synonym was used in 1964 by Weidel and Pelzer [1]. Peptidoglycan is present in the outer layer of the cytoplasmic membrane and its structure. The structure of peptidoglycan depends on the bacteria strain. It is estimated that in Gram-negative bacteria, it occupies only about 10–20% of the total area of the cell wall, when in Gram-positive bacteria it is 50 and up to 90% of all space. Problems with isolation with high purity of biological material shows the need for developing techniques for chemical synthesis of peptidoglycan fragments and their analogs. In past few years there has been a growing interest within the synthesis of compounds glycoprotein (glycopeptides, peptidoglycan, etc.). As a basis for the construction of cell walls of many bacteria. Despite intensive research and gain significant knowledge of the physical and biological, chemical synthesis or biosynthesis (Fig. 5 and 6) of peptidoglycan, not so far failed to unambiguously determine its three-dimensional structure. The works of Kelman and Rogers [15] and Dimitriev [20] nearer picture of its structure. However, the time to develop in vivo visualization of cell structure it will be difficult to identify correctly peptidoglycan three-dimensional structure. Due to the important biological roles of murein, many research centers have taken to attempt their chemical synthesis. For biological research began to use chemically synthesized peptidoglycan fragments which guaranteed both uniform and a certain structure. An important roles in the development of methods of chemical synthesis of peptidoglycan had H. Chowdhury work, Fig. 8 [35], Hesek, Fig. 9 and 10 [36, 37], Dziarskiego [38] and Boneca [39] and Inamury [34, 40].
Rocznik
Strony
513--540
Opis fizyczny
Bibliogr. 41 poz., schem.
Twórcy
  • Uniwersytet Gdański, Wydział Chemii, Pracownia Chemii Cukrów ul. Wita Stwosza 63, 80-303 Gdańsk
  • Uniwersytet Gdański, Wydział Chemii, Pracownia Chemii Cukrów ul. Wita Stwosza 63, 80-303 Gdańsk
autor
  • Uniwersytet Gdański, Wydział Chemii, Pracownia Chemii Cukrów ul. Wita Stwosza 63, 80-303 Gdańsk
Bibliografia
  • [1] W. Weidel, H. Pelzer, Adv. Enzymol. RAMB, 1964, 26, 193.
  • [2] a) W.W. Navarre, O. Schneewind, Microbiology and Molecular Biology Reviews, 1999, 63, 174; b) A.K. Rai, S.B. Rai, D.K. Rai, Journal of Molecular Structure (Theochem), 2003, 626, 53; c) J. Heijenoort, Glycobiology, 2001, 11, 25R; d) N. Kubasch, R.R. Schmidt, Eur. J. Org. Chem., 2002, 2710.
  • [3] S. Inamura, Y. Fujimoto, A. Kawasaki, Z. Shiokawa, E. Woelk, H. Heine, B. Lindner, N. Inohara, S. Kusumoto, K. Fukase, Org. Biomol. Chem., 2006, 4, 232.
  • [4] a) S. Bauer, C.J. Kirchning, H. Hacker, V. Redecke, S. Hausmann, S. Akira, H. Wagner, G.B. Lipford, Proc. Natl. Acad. Sci. U. S. A., 2001, 98, 9237; b) A.J. Ulmer, T.E. Rietschel, H. Heine, Trends Glycosci. Glycotechnol., 2002, 14, 53.
  • [5] a) B. Pulendran, K. Palucka, J. Banchereau, Science, 2001, 293, 253; b) R. Medzhitov, C.A. Janeway Jr., Science, 2002, 296, 298; Chem., 1973, 27, 349.
  • [6] T.E. Rietschel, J. Schletter, B. Weidemann, V. El-Samalouti, U.Z.T. Mattern, U. Seydel, H. Brade, D.H. Flad, S. Kusumoto, D. Guta, R. Dziarski, J.A. Ulmer, Microb. Drug Resist., 1998, 4.
  • [7] A.M. Kołodziejczyk, A.S. Kołodziejczyk, Post. Bioch., 1987, 33, 203.
  • [8] K. Dzierzbicka, A.M. Kołodziejczyk, Polish J. Chem., 2003, 77, 373.
  • [9] F. Ellouz, A. Adam, R. Ciorbaru, E. Lederer, Biochem. Biophys. Res. Commun., 1974, 59, 1317.
  • [10] a) A. Adam, E. Lederek, Med. Res. Rev., 1984, 4, 111; b) A. Adam, E. Lederer, Immunology, 1988, 1, 205; c) J.P. Devlin, K.D. Hargrave, Tetrahedron, 1989, 45, 4327; d) A. Hasegawa, H. Okumura, M. Kiso, Res. Bull. Fac. Arg. Gifu University, 1979, 42, 169; C.A., 93, 239878z (1980); e) K. Matsumoto, H. Ogawa, T. Kusama, O. Nagase, N. Sawaki, M. Inage, S. Kusumoto, T. Shiba, I. Azuma, Infect. Immun., 1981, 32, 748; g) S. Kusumoto, M. Inage, T. Shiba, I. Azuma, Y. Yamamura, Tetrahedron Lett., 1978, 49, 4899.
  • [11] a) A. Arendt, A.M. Kołodziejczyk, T. Sokołowska, Rocz. Chem., 1972, 46, 1707; b) A. Arendt, A.M. Kołodziejczyk, T. Sokołowska, Rocz. Chem., 1974, 48, 1707.
  • [12] A. Arendt, A.M. Kołodziejczyk, T. Sokołowska, Pol. J. Chem., 1974, 48, 1921.
  • [13] S. Kobayashi, T. Fukuda, H. Yukimasa, M. Fujino, I. Azuma, Y. Yamamura, Bull. Chem. Soc. Jpn., 1984, 57, 3182.
  • [14] K. Dzierzbicka, A.M. Kołodziejczyk, J. Med. Chem., 2001, 44, 3606; K. Dzierzbicka, P. Trzonkowski, P. Sewerynek, A. Myśliwski, J. Med. Chem., 2003, 46, 978.
  • [15] a) H. Formanek, S. Formanek, H. Wawra, Eur. J. Biochem., 1974, 46, 279; b) H. Formanek, K.H. Schleifer, H.P. Seidel, FEBS Lett., 1976, 70, 150; c) M.V. Kelemen, H. Rogers, J. Proc. Natl. Acad. Sci. USA, 1971, 68, 992.
  • [16] a) H. Labischinski, G. Barnickel, H. Bradaczek, P. Giesbrecht, Eur. J. Biochem., 1979, 95, 147; b) H. Labischinski, G. Barnickel, D. Naumann, P. Keller, Ann. Inst. Pasteur Microbiol., 1985, 136A, 45.
  • [17] H. Labischinski, H. Maidhof, Bacterial peptidoglycan: overview and evolving concepts, [w:] J.M. Ghuysen, R. Hackenbeck (Red.), Bacterial cell wall, Elsevier Science B.V., Amsterdam, The Netherlands., 1994, 23.
  • [18] D. Gally, A.R. Archibald, J. Gen. Microbiol., 1993, 139, 1907.
  • [19] M.A. Snowden, H.R. Perkins, A.W. Wyke, M.V. Hayes, J.B. Ward, J. Gen. Microbiol., 1989, 135, 3015.
  • [20] B.A. Dmitriev, F.V. Toukach, O. Holst, E.T. Rietschel, S. Ehlers, Journal of Bacteriology, 2004, 186, 7141.
  • [21] J.T. Park, J. Biol. Chem., 1952, 194, 877.
  • [22] J. van Heijenoort, Nat. Prod. Rep., 2001, 18, 503.
  • [23] a) Z. Markiewicz, Z.A. Kwiatkowski, Bakterie Antybiotyki Lekooporność, 2008, Wydawnictwo Naukowe PWN; b) J. van Heijenoort, [w:] Bacterial Cell Wall, J.-M. Ghuysen, R. Hakenbeck (Red.), Elsevier Science B.V., Amsterdam, 1994, 39.
  • [24] M. Ge, Z. Chen, R. Onishi, J. Kohler, L.L. Silver, R. Kerns, S. Fukuzawa, Ch. Thompson, D. Kahne, Science, 1999, 284, 507.
  • [25] a) C. Goffin, J.-M. Ghuysen, Microbiol. Mol. Biol. Rev., 1998, 62, 1079; b) J. van Heijenoort, Glycobiology, 2001, 11, 25R.
  • [26] a) M. Matsuhashi, in Bacterial Cell Wall, ed. J.-M. Ghuysen and R. Hakenbeck, Elsevier Science B.V., Amsterdam, 1994, 55; b) J.-M. Ghuysen, G. Dive, [w:] Bacterial Cell Wall, J.-M. Ghuysen, R. Hakenbeck (Red.), Elsevier Science B.V., Amsterdam, 1994, 103.
  • [27] H.M. Pooley, D. Karamata, In Bacterial Cell Wall, J.-M. Ghuysen R. Hakenbeck (Red.), Elsevier Science B.V., Amsterdam, 1994, 187.
  • [28] C.R.H. Raetz, [w:] Escherichia coli and Salmonella: Cellular and Molecular Biology, F.C. Neidhardt, R. Curtis III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Red.), ASM Press, Washington, D.C., 1996, 1035.
  • [29] P.D. Rick, R.P. Silver, [w:] Escherichia coli and Salmonella: Cellular and Molecular Biology, F.C. Neidhardt, R. Curtis III, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, H.E. Umbarger (Red.), ASM Press, Washington, D.C., 1996, 104.
  • [30] R.J. White, Biochem. J., 1968, 106, 847.
  • [31] H.C. Wu, T.C. Wu, J. Bacteriol., 1971, 105, 455.
  • [32] L. Jolly, S. Wu, J. van Heijenoort, H. de Lencastre, D. Mengin-Lecreulx, A. Tomasz, J. Bacteriol., 1997, 179, 5321.
  • [33] P. Glanzmann, J. Gustafson, H. Komatsuzawa, K. Ohta, B. Berger-Bāchi, Antimicrob. Agents Chemother., 1999, 262, 202.
  • [34] S. Inamura, K. Fukase, S. Kusumoto, Tetrahedron Lett., 2001, 42, 7613.
  • [35] A.R. Chowdhury, A. Siriwardena, G.J. Boons, Tetrahedron Lett., 2002, 43, 7805.
  • [36] D. Hesek, M. Lee, K. Morio, S. Mobashery, J. Org. Chem., 2004, 69, 2137.
  • [37] C. Fuda, D. Hesek, M. Lee, K. Morio, T. Nowak, Sh. Mobashery, J. Am. Chem. Soc., 2005, 127, 2056.
  • [38] R. Dziarski, D. Gupta, Infect. Immun., 2005, 73, 5212.
  • [39] L.H. Travassos, S.E. Girardin, D.J. Philpott, D. Blanot, M.A. Nahori, C. Werts, I.G. Boneca, EMBO Rep., 2004, 5, 1000.
  • [40] S. Inamura, Y. Fujimoto, A. Kawasaki, Z. Shiokawa, E. Woelk, H. Heine, B. Lindner, N. Inohara, S. Kusumoto, K. Fukase, Org. Biomol. Chem., 2006, 4, 232.
  • [41] M.S. VanNieuwenhze, S.C. Mauldin, M. Zia-Ebrahimi, B.E. Winger, W.J. Hornback, Sh.L. Saha, J.A. Aikins, L.C. Blaszczak, J. Am. Chem. Soc., 2002, 124, 3656.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-1c533c39-511c-4c66-bf60-4dd81f32c238
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.