Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides
Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides(411 views) Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R, Rossi F
Keywords: α2-Helix, β-Sheet, Amyloid, Cd Titration, Encephalopathies, Nmr Structure, Prion Protein, Prion Toxicity, Transmissible Spongiform, Dodecyl Sulfate, Threonine, Alpha Helix, Article, Beta Sheet, Carboxy Terminal Sequence, Circular Dichroism, Nuclear Magnetic Resonance, Peptide Synthesis, Priority Journal, Protein Conformation, Protein Folding, Structure Activity Relation, Humans, Magnetic Resonance Spectroscopy, Neurotoxins, Protein Structure, Secondary, Tertiary, Trifluoroethanol, Water,
Affiliations: *** IBB - CNR ***
Dipartimento delle Scienze Biologiche, C.I.R.Pe.B., Università Federico II di Napoli, Via Mezzocannone 16, 80134 Naples, Italy
Dipartimento de Scienze e Tecnologie per l'Ambiente e Il Territorio, Università del Molise, Pesche, Italy
Istituto di Chimica Biomolecolare, CNR, Pozzuoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Naples, Italy
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L pez Garcia, F., Zahn, R., Riek, R., W thrich, K., NMR structure of the bovine prion protein (2000) Proc. Natl. Acad. Sci. U. S. A, 97, pp. 8334-8339
P rez, D. R., W thrich, K., NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226) (2005) J. Biomol. NMR, 31, pp. 260-260
Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., W thrich, K., Prion protein NMR structures of cats, dogs, pigs, and sheep (2005) Proc. Natl. Acad. Sci. U. S. A, 102, pp. 640-645
Gossert, A. D., Bonjour, S., Lysek, D. A., Fiorito, F., W thrich, K., Prion protein NMR structures of elk and of mouse/elk hybrids (2005) Proc. Natl. Acad. Sci. U. S. A, 102, pp. 646-650
Prusiner, S. B., Prions (1998) Proc. Natl. Acad. Sci. U. S. A, 95, pp. 13363-13383
Kelly, J. W., The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways (1998) Curr. Opin. Struct. Biol, 8, pp. 101-106
Scott, M. R., Will, R., Ironside, J., Nguyen, H. -O. B., Tremblay, P., DeArmond, S. J., Prusiner, S. B., Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans (1999) Proc. Natl. Acad. Sci. U. S. A, 96, pp. 15137-15142
Jackson, G. S., Hosszu, L. L., Power, A., Hill, A. F., Kenney, J., Saibil, H., Craven, C. J., Collinge, J., Reversible conversion of monomeric human prion protein between native and fibrillogenic conformations (1999) Science, 283, pp. 1935-1937
Bosques, C. J., Imperiali, B., The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment (2003) Proc. Natl. Acad. Sci. U. S. A, 100, pp. 7593-7598
Brown, D. R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., Copper (II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper (II) and the binding motif in C-terminal protein region (2004) J. Inorg. Biochem, 98, pp. 133-143
DuBay, K. F., Pawar, A. P., Chiti, F., Zurdo, J., Dobson, C. M., Vendruscolo, M., Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains (2004) J. Mol. Biol, 341, pp. 1317-1326
Galzitskaya, O. V., Garbuzynskiy, S. O., Lobanov, M. Y., Prediction of amyloidogenic and disordered regions in protein chains (2006) PLoS Comput. Biol, 2, pp. 1639-1648
Dima, R. I., Thirumalai, D., Exploring the propensities of helices in PrPC to form sheet using NMR structures and sequence alignments (2002) Biophys. J, 83, pp. 1268-1280
Prusiner, S. B., Molecular biology and pathogenesis of prion diseases (1996) Trends Biochem. Sci, 21, pp. 482-487
Shamsir, M. S., Dalby, A. R., One gene, two diseases and three conformations: Molecular dynamics simulations of mutants human prion protein at room temperature and elevated temperatures (2005) Proteins, 59, pp. 275-290
Cobb, N. J., S nnichsen, F. D., McHaourab, H., Surewicz, W. K., Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure (2007) Proc. Natl. Acad. Sci. U. S. A, 104, pp. 18946-18951
Wu, C. S., Ikeda, K., Yang, J. T., Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution (1981) Biochemistry, 20, pp. 566-570
Wu, C. S., Yang, J. T., Sequence-dependent conformations of short polypeptides in a hydrophobic environment (1981) Mol. Cell. Biochem, 40, pp. 109-122
W thrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley: New York
G ntert, P., Braun, W., W thrich, K., Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA (1991) J. Mol. Biol, 217, pp. 517-530
G ntert, P., Mumenthaler, C., W thrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) J. Mol. Biol, 273, pp. 283-298
Bordbar, A. K., Saboury, A. A., Housaindokht, M. R., Moosavi-Movahedi, A. A., Statistical effects of the binding of ionic surfactant to protein (1997) J. Colloid Interface Sci, 192, pp. 415-419
Cox, D. L., Pan, J., Singh, R. R. P., A mechanism for copper inhibition of infectious prion conversion (2006) Biophys. J, 91, pp. L11-L13
Haire, L. F., Whyte, S. M., Vasisht, N., Gill, A. C., Verma, C., Dodson, E. J., Dodson, G. G., Bayley, P. M., The crystal structure of the globular domain of sheep prion protein (2004) J. Mol. Biol, 336, pp. 1175-1183
Knaus, K. J., Morillas, M., Swletnicki, W., Malone, M., Surewicz, W. K., Yee, V. C., Crystal structure of the human prion protein reveals a mechanism for oligomerization (2001) Nat. Struct. Biol, 8, pp. 770-774
Jackson, G. S., Collinge, J., The molecular pathology of CJD: Old and new variants (2001) Mol. Pathol, 54, pp. 393-399
Fitzmaurice, T. J., Burke, D. F., Hopkins, L., Yang, S., Yu, S., Sy, M. -S., Thackray, A. M., Bujdoso, R., The stability and aggregation of ovine prion protein associated with classical and atypical scruple correlates with the case of unwinding of helix-2 (2008) Biochem J, 409, pp. 367-375
Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides
Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides
No results.
Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides