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Metody chemicznej ligacji w syntezie peptydów i białek. Część 1

Treść / Zawartość
Identyfikatory
Warianty tytułu
EN
Chemical ligation methods in the synthesis of peptides and proteins. Part 1
Języki publikacji
PL
Abstrakty
EN
Proteins are biological macromolecules affecting very important functions in the body. They are involved in many biochemical processes. They can perform catalytic functions acting as enzymes. They also participate in the transport of many small molecules and ions – for example one molecule of hemoglobin carries four molecules of oxygen. In addition, proteins serve as antibodies and are involved in transmission of nerve impulses as receptor proteins. Because peptides and proteins perform so important functions, to study them it is essential to obtain these compounds in the greatest possible amounts. The compounds can be obtained generally by three main methods: • by isolation of the native peptides and proteins • by expression in microorganisms • by chemical synthesis. Each of the above methods has its advantages and disadvantages, but only the chemical synthesis gives the possibility to introduce modifications to the structure of the resulting protein, such as the insertion of new functional groups, to give the product in the final form and with satisfactory yield. In this review we present the application of chemical ligation methods in the synthesis of peptides and proteins. We describe in details mechanism of native chemical ligation method and the conditions necessary to carry the reaction [1]. The synthesis of long polypeptide chains by kinetically controlled ligation (KCL) is also depicted [2]. This part of the paper also details a number of approaches to noncysteine containing peptides by chemical ligation methods.
Rocznik
Strony
727--746
Opis fizyczny
Bibliogr. 30 poz., schem.
Twórcy
  • Katedra Chemii Biomedycznej, Wydział Chemii, Uniwersytet Gdański, ul. Wita Stwosza 63, 80-308 Gdańsk
  • Katedra Chemii Biomedycznej, Wydział Chemii, Uniwersytet Gdański, ul. Wita Stwosza 63, 80-308 Gdańsk
  • Katedra Chemii Biomedycznej, Wydział Chemii, Uniwersytet Gdański, ul. Wita Stwosza 63, 80-308 Gdańsk
Bibliografia
  • [1] L. Raibaut, N. Ollivier, O. Melnyk, Chem. Soc. Rev., 2012, 41, 7001.
  • [2] J. Lee, Y. Kwon, B.N. Pentelute, D. Bang, Bioconjugate Chem., 2011, 22, 1645.
  • [3] R.B. Merrifield, J. Am. Chem. Soc., 1963, 85, 2149.
  • [4] J.P. Tam, J. Xu, K.D. Eom, Biopolymers (Peptide Science), 2001, 60, 194.
  • [5] P.E. Dawson, T.W. Muir, I. Clark-Lewis, S.B.H. Kent, Science, 1994, 266, 776.
  • [6] H.P. Hemantha, N. Narendra, V.V. Sureshbabu, Tetrahedron, 2012, 68, 9491.
  • [7] C.P.R. Hackenberger, D. Schwarzer, Angew. Chem. Int. Ed., 2008, 47, 10030.
  • [8] S.B.H. Kent, Chem. Soc. Rev., 2009, 38, 338.
  • [9] F.I. Valiyaveetil, R. MacKinnon, T.W. Muir, J. Am. Chem. Soc., 2002, 124, 9113.
  • [10] E.C.B. Johnson, S.B.H. Kent, J. Am. Chem. Soc, 2006, 128, 6640.
  • [11] T.M. Hackeng, J.H. Griffin, P.E. Dawson, Proc. Natl. Acad. Sci. USA, 1999, 96, 10068.
  • [12] D. Bang, B.L. Pentelute, S.B.H. Kent, Angew. Chem. Int. Ed., 2006, 45, 3985.
  • [13] M. Villain, J. Vizzarone, K. Rose, Chem. Biol., 2001, 8, 673.
  • [14] T. Durek, V.Y. Torbeev, S.B.H. Kent, Proc. Natl. Acad. Sci. USA, 2007, 104, 4846.
  • [15] V.Y. Torbeev, S.B.H. Kent, Angew. Chem. Int. Ed. 2007, 46, 1667.
  • [16] P.W.R. Harris, M.A. Brimble, Biopolymers (Peptide Science), 2015, 104, 116.
  • [17] F.R. Naider, J.M. Becker, Biopolymers, 1997, 43, 3.
  • [18] L. Zhang, J.P. Tam, Tetrahedron Lett., 1997, 38, 3.
  • [19] R. Yang, L. Qi, Y. Liu, Y. Ding, M.S.Y. Kwek, C.-F. Liu, Tetrahedron Lett., 2013, 54, 3777.
  • [20] D. Macmillan, L. Arham, J. Am. Chem. Soc., 2004, 126, 9530.
  • [21] L.Z. Yan, P.E. Dawson, J. Am. Chem. Soc., 2001, 123, 526.
  • [22] Q. Wan, S.J. Danishefsky, Angew. Chem. Int. Ed. Engl., 2007, 46, 9248.
  • [23] J. Chen, Q. Wan, Y. Yuan, J. Zhu, S.J. Danishefsky, Angew. Chem. Int. Ed. Engl., 2008, 47, 8521.
  • [24] D. Crich, A. Banerjee, J. Am. Chem. Soc., 2007, 129, 10064.
  • [25] R.L. Heinrikson, J. Biol. Chem., 1971, 246, 4090.
  • [26] D. Macmilan, Angew. Chem. Int. Ed., 2006, 45, 7668.
  • [27] T. Kawakami, S. Aimoto, Tetrahedron Lett., 2003, 44, 6059.
  • [28] L.E. Canne, S.J. Bark, S.B.H. Kent, J. Am. Chem. Soc., 1996, 118, 5891.
  • [29] S.F. Loibl, Z. Harpaz, O. Seitz, Angew. Chem. Int. Ed., 2015, 54, 15055.
  • [30] C. Rao, C.- F. Liu, Org. Biomol. Chem., 2017, 15, 2491.
Uwagi
Opracowanie rekordu w ramach umowy 509/P-DUN/2018 ze środków MNiSW przeznaczonych na działalność upowszechniającą naukę (2018).
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-bba4f3bd-b50b-4f66-b2cc-89323b688792
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