Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals(382 views) Pietropaolo A, Muccioli L, Zannoni C, Rizzarelli E
Dipartimento di Chimica Fisica ed Inorganica and INSTM, Universita di Bologna, V.le Risorgimento, 4, I-40136 Bologna, Italy.
Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 1-95125 Catania, Italy
References: Prusiner, S.B., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 13363-1338
Chiesa, R., Harris, D.A., (2009) PLoS Biol, 7, pp. e75
Wopfner, F., Weidenhofer, G., Schneider, R., von Brunn, A., Gilch, S., Schwarz, T.F., Werner, T., Schatzl, H.M., (1999) J. Mol. Biol, 289, pp. 1163-1178
Harris, D.A., Falls, D.L., Johnson, F.A., Fischbach, G.D., (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 7664-7668
Mendola, D.L., Pietropaolo, A., Pappalardo, G., Zannoni, C., Rizzarelli, E., (2008) Curr. Alzheimer Res, 5, pp. 579-590
Collinge, J., Clarke, A.R., (2007) Science, 318, pp. 930-936
Zahn, R., Liu, A., Lührs, T., Riek, R., von Schroetter, C., Garcìa, F.L., Billeter, M., Wüthrich, K., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 145-150
Calzolai, L., Lysek, D.A., Perez, D.R., Guntert, P., Wüthrich, K., (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 651-655
Nunziante, M., Gilch, S., Schätzl, H.M., (2003) J. Biol. Chem, 278, pp. 3726-3734
Frankenfield, K.N., Powers, E.T., Kelly, J.W., (2005) Protein Sci, 14, pp. 2154-2166
Butowt, R., Davies, P., Brown, D.R., (2007) J. Neurosci. Res, 85, pp. 2567-2579
Shyng, S.L., Moulder, K.L., Lesko, A., Harris, D.A., (1995) J. Biol. Chem, 270, pp. 14793-14800
Pietropaolo, A., Raiola, L., Muccioli, L., Tiberio, G., Zannoni, C., Fattorus-so, R., Isernia, C., Rizzarelli, E., (2007) Chem. Phys. Lett, 442, pp. 110-118
Pietropaolo, A., Muccioli, L., Zannoni, C., La Mendola, D., Maccarrone, G., Pappalardo, G., Rizzarelli, E., (2008) J. Phys. Chem. B, 112, pp. 5182-5188
Langella, E., Improta, R., Barone, V., (2004) Biophys. J, 87, pp. 3623-3632
De Simone, A., Dodson, G.G., Verma, C.S., Zagari, A., Fraternali, F., (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 7535-7540
Pappalardo, M., Milardi, D., Grasso, D., La Rosa, C., (2007) New J. Chem, 31, pp. 901-905
Ji, H.F., Zhang, H.Y., (2007) Biochem. Biophys. Res. Commun, 359, pp. 790-794
Bonomo, R.P., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., Tabbí, G., (2000) Chem. Eur. J, 6, pp. 4195-4202
Bonomo, R.P., Cucinotta, V., Giuffrida, A., Impellizzeri, G., Magri, A., Pappalardo, G., Rizzarelli, E., Vagliasindi, L.I., (2005) Dalton Trans, pp. 150-158
Di Natale, G., Grasso, G., Impellizzeri, G., La Mendola, D., Micera, G., Mihala, N., Nagy, Z., Sóvágó, I., (2005) Inorg. Chem, 44, pp. 7214-7225
La Mendola, D., Bonomo, R.P., Impellizzeri, G., Maccarrone, G., Pappalardo, G., Rizzarelli, A.P.A.E., Zito, V., (2005) J. Biol. Inorg. Chem, 10, pp. 463-475
Ösz, K., Nagy, Z., Pappalardo, G., Natale, G.D., Micera, D.S.G., Rizzarelli, E., Sóvágó, I., (2007) Chem. Eur. J, 13, pp. 7129-7143
Gaggelli, E., Kozlowski, H., Valensin, D., Valensin, G., (2006) Chem. Rev, 106, pp. 1995-2044
Bonomo, R.P., Di Natale, G., Rizzarelli, E., Tabbí, G., (2009) Dalton Trans, pp. 2637-2646
Jackson, G., Murray, I., Hosszu, L.L.P., Gibbs, N., Waltho, J.P., Clarke, A., Collinge, J., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 8531-8535
Brown, D.R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., (2004) J. Inorg. Biochem, 98, pp. 133-143
Marcotte, E.M., Eisenberg, D., (1999) Biochemistry, 38, pp. 667-676
Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals
We investigate the conformations of the full chicken prion protein (ChPrP1-267) in solution at neutral pH with molecular dynamics simulations. We focus on the persistence of its secondary structure motifs using a recently proposed protein chirality indicator [A. Pietropaolo et al., Proteins 2008, 70, 667-677]. From this, we find a high rigidity of helix 2 (ChPrP178-195) and of the hexarepeat domain, which is turn rich, and a plasticity of the short beta-sheet, consistent with the available NMR structural details. We also determine the extent of solvation for each residue, revealing local minima for such structured regions. These features hint at a possible origin of the high resistance to proteolysis of the avian prion proteins and of its capability in preventing the aggregation in comparison to mammals.
Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(357 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(449 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote