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Od białek amyloidogennych do nanostruktur tworzonych przez proste peptydy

Identyfikatory
Warianty tytułu
EN
From amyloidogenic proteines to nanostructures formed by simple peptides
Języki publikacji
PL
Abstrakty
EN
Molecular self-assembly offers unique opportunity for the fabrication of novel supramolecular structures and advanced materials. The inspiration for the development of such structures is often resulting from self-assembling modules in biology, as natural systems always form complex structures from relatively simple building blocks [1, 2]. Several studies had demonstrated the versatility of peptide to form well organized assemblies. This includes cyclic peptides designed with alternating D- and L-amino acids, amphiphile peptides, peptide-conjugates and ionic self-complementary peptides. The 37-residue amylin (Fig. 5), also known as islet amyloid polypeptide, forms fibrils that are the main component of amyloid that develops in the pancreas of type 2 diabetes patients. Amylin also in vitro readily forms amyloid fibrils that are highly polymorphic under typical experimental conditions [21-33]. The molecular structure of amylin protofilaments in striated ribbons closely resembles the protofilament in amyloid fibrils with a similar morphology formed by the 40-residue beta-amyloid peptide that is associated with Alzheimer's disease [48-54]. But not only amylin is a self-assembling peptide. We can also find another examples in biological proteins and peptides that have the intrinsic ability to selfassemble into elongated solid nanofibrils, which may give rise to amyloid diseases or alternatively, inspire applications ranging from tissue engineering to nanoelectronics (Fig. 4). Proteinaceous fibrils are extensively studied searching for detailed theoretical models explaining the mechanism of formation, morphology and properties of self-assembled structures. Especially intriguing state of protein-like selfassemblies are nanotubes (NTs), defined as an elongated nano-object with a definite inner hole. In contrast to proteinaceous fibrils, nanotubes are much less frequently observed and far less well understood. However, they have attracted research interest as key components for nanotechnology (Fig. 13). The simplest objects prone to self-assembly are aromatic dipeptides diphenylalanine, diphenylglycine, and their simple derivatives form nanotubes or spherical nanometric assemblies. Remarkable flexibilities of peptides fragments in formation of nanostructures recently have been considered important for many applications in various fields including molecular electronics, tissue engineering, and material science [87-92].
Rocznik
Strony
645--671
Opis fizyczny
Bibliogr. 92 poz., rys., tab., wykr.
Twórcy
Bibliografia
  • [1] M. Reches, E. Gazit, Science, 2003, 300, 625.
  • [2] H. Matsui, B. Gologan, S. Pan, Eur. Phys. J. D., 2001, 16, 403.
  • [3] G. Colombo, P. Soto, E. Gazit, Trends Biotechnol., 2006, 25, 211.
  • [4] C.M. Dobson, Nature, 2002, 418, 729.
  • [5] F. Chiti, C.M. Dobson, Annu. Rev. Biochem., 2006, 75, 333.
  • [6] M.R. Chapman, S.R. Lloyd, S.P. Jerome, R.J.H. Robyn, H. Marten, S. Normark, J.H. Scott, Science, 2002, 295, 851.
  • [7] M. Lopez de la Paz, E. Lacroix, M. Ramírez-Alvarado, L. Serrano, Proc. Natl. Acad. Sci. U. S. A., 2002, 99, 16052.
  • [8] T. Konno, K. Murata. K. Nagayama, FEBS Lett., 1999, 454, 122.
  • [9] (a) S.B. Prusiner, Prions. Proc. Natl Acad. Sci. USA, 1998, 95, 13363. (b) J.D. Harper, P.T. Lansbury, Annu. Rev. Biochem., 1997, 66, 385. (c) F.E. Cohen, S.B. Prusiner, Annu. Rev. Biochem., 1998, 67, 793. (d) S.B. Prusiner, M.R. Scott, S.J. DeArmond, F.E. Cohen, Cell, 1998, 93, 337. (e) A. Aguzzi, F. Montrasio, P.S. Kaeser, Cell, 1998, 93, 337.
  • [10] (a) S. Dealler, R. Lacey, Nutr. Health, 1991, 3, 117. (b) R.A. Moore, I. Vorberg, S.A. Priola, Arch Virol Suppl., 2005, 19, 187.
  • [11] G.S. Jackson, A.R. Clarke, Curr. Opin. Struct. Biol., 2000, 10, 69.
  • [12] (a) B.S. Cox, M.F. Tuite, C.S. McLaughin, Yeast, 1988, 4, 159. (b) B.S. Cox, M.F. Tuite, C.J. Mundy, Genetics, 1980, 95, 589.
  • [13] R.B. Wickner, Science, 1994, 264, 566.
  • [14] I. Stansfield, K.M. Jones, V.V. Kushnirov, A.R. Dagkesamanskaya, A.I. Poznyakovski, S.V. Paushkin, C.R. Nierras, B.S. Cox, M.D. Ter-Avanesyan, M.F. Tuite, EMBO J., 1995, 14, 4365.
  • [15] (a) M. Balbirnie, R.Grothe, D.S. Eisenberg, Proc. Natl Acad. Sci. USA, 2001, 98, 2375. (b) R. Diaz-Avalos, C. Long, E. Fontano, M. Balbirnie, R. Grothe, D. Eisenberg, D.L.D. Caspar, J. Mol. Biol., 2003, 330, 1165.
  • [16] M.D. Michelitsch, J.S. Weissman, Proc. Natl Acad. Sci., 2001, 97, 11910.
  • [17] (a) M.F. Perutz, T. Johnson, M. Suzuki, J.T. Finch, Proc. Natl Acad. Sci., 1994, 91, 5355. (b) K. Stott, J.M. Blackburn, P.J.G. Butler, M.F. Perutz, Proc. Natl Acad. Sci. 1999, 92, 6509. (c) M.F. Perutz, B.J. Pope, D. Owen, E.E. Wanker, E. Scherzinger, Proc. Natl Acad. Sci., 2002, 99, 5596.
  • [18] J. Lipfert, J. Franklin, F. Wu, S. Doniach, J. Mol. Biol., 2005, 349, 648.
  • [19] M. Reches, Y. Porat, E. Gazit, J. Biol. Chem., 2002, 277, 35475.
  • [20] G.M. Whitesides, J.P. Mathias, C.T. Seto, Science, 1991, 254, 1312.
  • [21] N. Vaysse, Pancreatology, 2005, 5, 27.
  • [22] D. Porte, S.E. Kahn, Diabetes, 2001, 50, 160.
  • [23] T.R. Rink, K. Beaumont, J. Koda, A. Young, Trends Pharmacol. Sci., 1993, 14, 113.
  • [24] R.L. Hul, G.T. Westermark, P. Westermark, S.E. Kahn, J. Clin. Endocrinol. Metab., 2004, 89, 3629.
  • [25] S.L. Aronoff, K. Berkowitz, B. Shreiner, L. Want, Diabetologia po Dyplomie, 2004, 1, 49.
  • [26] J.B. Buse, C. Weyer, D.G. Maggs, Clinical Diabets, 2002, 20, 137.
  • [27] J. Pullman, T. Darsow, J.P. Frias, Vasc. Health Risk Manag., 2006, 2, 203.
  • [28] L.L. Want, R.E. Ratner, Curr. Diab. Rep., 2006, 6, 344.
  • [29] J. McQueen, Am. J. Health Syst. Pharm., 2005, 62, 2363.
  • [30] R. Ratner, F. Whitehouse, M.S. Fineman, S. Strobel, L. Shen, D.G. Maggs, C. Weyer,G.C. Kolterman, Exp. Clin. Endocrinol. Diabetes, 2005, 113, 199.
  • [31] F. Whitehouse, D.F. Kruger, M. Fineman, L. Shen, S.L. Aronoff, S.V. Edelman, J. Crean, Y. Wang, D.G. Maggs, O.G. Kolterman, M. Chandran, S.R. Mudaliar, Diabetes Care, 2002, 25, 724.
  • [32] D.F. Kruger, M.A. Gloster, Drugs, 2004, 64, 1419.
  • [33] R.E. Ratner, R. Dickey, M. Fineman, D.G. Maggs, L. Shen, S.T. Strobel, C. Weyer, G.C. Kolterman, Diabet. Med., 2004, 21, 1204.
  • [34] R. Guthrie, D.M. Karl, Y. Wang, G. Lorenzi, Diabetes, 2005, 54, 478-P.
  • [35] M. Stadler, C. Anderwald, T. Karer, A. Tura, T. Kastenbauer, M. Auinger, Diabetes Care, 2006, 29, 1031.
  • [36] A.R. Philips, R. Anthony, F.M. Abu-Zidan, M. Fikri, M.J. Bonham, J.D. Martin, G.J. Cooper, J.S. Garth, J.A. Windsor, A. John, Pancreas, 2000, 20, 105.
  • [37] A. Novials, L. Rodriguez-Manas, A. Chico, M. El Assar, C. Sílvia, G. Ramon, J. Clin. Endocrinol. Metab., 2007, 92, 1446.
  • [38] P.A. Rushing, M.M. Hagan, R.J. Seeley, T.A. Lutz, S.C. Woods, Endocrinology, 2000, 141, 850.
  • [39] W. Gong, Z.H. Liu, C.H. Zeng, A. Peng, H.P. Chen, H. Zhou, L.S. Li, Kidney International, 2007, 72, 213.
  • [40] J.D. Harper, P.T. Lansbury, Jr. Annu. Rev. Biochem., 1997, 66, 385.
  • [41] B. Häggqvist, J. Näslund, K. Sletten, G.T. Westermark, G. Mucchiano, L.O. Tjernberg, C. Nordstedt, U. Engström, P. Westermark, Proc. Natl. Acad. Sci., 1999, 96, 8669.
  • [42] J.I. Guijarro, M. Sunde, J.A. Jones, I.D. Campbell, C.M. Dobson, Proc. Natl. Acad. Sci., 1998, 95, 4224.
  • [43] C.M. Dobson, Trends Biochem. Sci., 1999, 24, 329.
  • [44] E. Gazit, Angew. Chem. Int. Edit., 2002, 41, 257.
  • [45] J.C Rochet, P.T.Jr. Lansbury, Curr Opin Struct Biol., 2000, 10, 60.
  • [46] R. Kayed, E. Head, J.L. Thompson, T.M. McIntire, S.C. Milton, C.W. Cotman, C.G. Glabe, Science, 2003, 300, 486.
  • [47] J. McLaurin, D. Yang, C.M. Yip, P.E. Fraser, J Struci Biol., 2000, 130, 259.
  • [48] H. Lin, R. Bhatia, R. Lal, FASEB J., 2001, 15, 2433.
  • [49] C.M. Yip, J. McLaurin, Biophys. J., 2001, 80, 1359.
  • [50] I. Kracun, S. Kalanj, J. Talan-Hranilovic, C. Cosovic, Neurochem. Int., 1992, 20, 433.
  • [51] J.W. Pettegrew, K. Panchalingam, R.L. Hamilton, R.J. McClure, Neurochem. Res., 2001, 26, 771.
  • [52] A. Kakio, S. Nishimotom, K. Yanagisawa, Y. Kozutsumi, K. Matsuzaki, Biochemistry, 2002, 41, 7385.
  • [53] W. Gibson Wood, G.P. Eckert, U. Igbavboa, W.E. Muller, Biochim. Biophys. Acta, 2003, 1610, 281.
  • [54] M. Bokvist, F. Lindstrom, A. Watts, G. Grobner, J. Mol. Biol., 2004, 335, 1039.
  • [55] N. Sawamura, M. Morishima-Kawashima, H. Waki, K. Kobayashi, T. Kuramochi, M.P. Frosch, K. Ding, M. Ito, T.W. Kim, R.E. Tanzi, F. Oyama, T. Tabira, S. Ando, Y. Ihara, J. Biol. Chem., 2000, 275, 27901.
  • [56] J. McLaurin, T. Franklin, A. Chakrabartty, P.E. Fraser, J. Mol. Biol., 1998, 278, 183.
  • [57] W. Colon, J.W. Kell, Biochemistry, 1992, 15, 8654.
  • [58] L.C. Wu, B.A. Schulman, Z.Y. Peng, P.S. Kim, Biochemistry, 1996, 35, 859.
  • [59] J.L. Whittingham, D.J. Scott, K. Chance, A. Wilson, J. Finch, J. Brange, G. Guy Dodson, Mol. Biol., 2002, 31, 479.
  • [60] H. Zhao, E.K. Tuominen, P.K. Kinnunen, Biochemistry, 2004, 43, 10302.
  • [61] M. Zhu, P.O. Souillac, C. Ionescu-Zanetti, S.A. Carter, A.L. Fink, J. Biol. Chem., 2002, 277, 50914.
  • [62] G. Terlecki, Adv. Clin. Exp. Med., 2006, 15, 513.
  • [63] K. Tenidis, M. Waldner, J. Bernhagen, W. Fischle, M. Bergmann, M. Weber, M.L. Merkle, W. Voelter, H. Brunner, A. Kapurniotu, J. Mol. Biol., 2000, 295, 1055.
  • [64] P. Westermark, U. Engström, K.H. Johnson, G.T. Westermark, C. Betsholtz, Proc. Natl. Acad. Sci., 1990, 87, 5036.
  • [65] R. Kayed, J. Bernhagen, N. Greenfield, K. Sweimeh, H. Brunner, W. Voelter, A. Kapurniotu, J. Mol. Biol., 1999, 287, 781.
  • [66] J.W. Höppener, B. Ahren, C.J.N. Lips, Engl. J. Med., 2000, 343, 411.
  • [67] R. Azriel, E. Gazit, J. Biol. Chem., 2001, 276, 34156.
  • [68] E. Gazit, FASEB J., 2002, 16, 77.
  • [69] E. Gazit, Bioinformatics, 2002, 18, 880.
  • [70] Y. Mazor, S. Gilead, I. Benhar, E. Gazit, J. Mol. Biol., 2002, 322, 1013.
  • [71] M. Reches, E. Gazit, Amyloid, 2004, 11, 81.
  • [72] M. Reches, Y. Porat, E. Gazit, J. Biol. Chem., 2002, 277, 35475.
  • [73] L. Tjernberg, W. Hosia, N. Bark, J. Thyberg, J. Johansson, J. Biol. Chem., 2002, 277, 43243.
  • [74] S.K. Maji, D. Haldar, M.G.B. Drew, A. Banerjee, A.K. Das, A. Banerjee, Tetrahedron, 2004, 60, 3251.
  • [75] M. Reches, E. Gazit, Science, 2003, 300, 625.
  • [76] N. Kol, L. Adler-Abramovich, D. Barlam, R.Z. Shneck, E. Gazit, I. Rousso, Nano Lett., 2005, 5, 1343.
  • [77] a) M. Reches, E. Gazit, Isr. J. Chem., 2005, 45, 363. b) M. Reches, E. Gazit, Current Nanoscience, 2006, 2, 105.
  • [78] M. Reches, E. Gazit, Nano Lett. 2004, 4, 581.
  • [79] I. Daidone, F. Simona, D. Roccatano, R.A. Broglia, G. Tiana, G. Colombo, A. Di Nola, Proteins, 2004, 57, 198.
  • [80] S.D. Khare, F. Ding, K.N. Gwanmesia, N.V. Dokholyan, PLoS Comput. Biol., 2005, 1, 230.
  • [81] G. Wei, N. Mousseau, P. Derreumaux, Biophys. J., 2004, 87, 3648.
  • [82] S. Santini, N. Mousseau, P. Derreumaux, J. Am. Chem. Soc., 2004, 126, 11509.
  • [83] G. Favrin, A. Irbäck, S. Mohanty, Biophys. J., 2004, 87, 3657.
  • [84] G.A. Silva, G. Zhu, M.F. Mehler, P.C. Mabie, J.A. Kessler, Science, 2004, 303, 1352.
  • [85] T.C. Holmes, C.M. DiPersio, R.O. Hynes, X. Su, A. Rich, Proc. Natl. Acad. Sci. U.S.A., 2000, 97, 6728.
  • [86] R.G. Ellis-Behnke, Y-X. Liang, S-W. You, D.K.C. Tay, S. Zhang, K-F. So, G.E. Schneider, Proc. Natl. Acad. Sci. U.S.A., 2006, 2006, 5054.
  • [87] Z. Zhao, I.A. Banerjee, H. Matsui, J. Am. Chem. Soc., 2005, 127, 8930.
  • [88] M. Yemini, M. Reches, J. Rishpon, E. Gazit, Anal. Chem., 2005, 77, 5155.
  • [89] M. Reches, E. Gazit, Nature Nanotechnology, 2006, 1, 195.
  • [90] M. Han, X.H. Gao, J.Z. Su, S. Nie, Nat. Biotechnol., 2001, 19, 631.
  • [91] J.F. Smith, A. Craig, C.M. Dobson, M.E. Welland, Proc. Natl. Acad. Sci. U.S.A., 2006, 103, 15806.
  • [92] N. Kol, L. Adler-Abramovich, D. Barlam, Z. Roni, E. Gazit, Nano Lett., 2005, 5, 1343.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-article-BUS8-0005-0015
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