Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details
Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details(353 views visite) Osz K, Nagy Z, Pappalardo G, Di Natale G, Sanna D, Micera G, Rizzarelli E, Sóvágó I
Department of Inorganic and Analytical Chemistry, University of Debrecen, 4010 Debrecen, Hungary. CNR, Institute of Biostructures and Bioimaging, Vie A. Doria, 95125 Catania, Italy Department of Chemical Sciences, University of Catania, V.le A. Doria 6, 95125 Catania, Italy Department of Chemistry, University of Sassari, Via Vienna 2, 07100 of Sassari, Italy
References Riferimenti: Prusiner, S.B., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 13363-1338
Collinge, J., (2001) Annu. Rev. Neurosa, 24, pp. 519-550
Prusiner, S.B., (1982) Science, 216, pp. 136-144
Zahn, R., (2003) J. Mol. Biol, 334, pp. 477-488
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., Wüthrich, K., (1996) Nature, 382, pp. 180-182
Stahl, N., Borchelt, D.R., Hsiao, K., Prusiner, S.B., (1987) Cell, 51, p. 229240
Kramer, M.L., Kratzin, H.D., Schmidt, B., Römer, A., Windl, O., Liemann, S., Hornemann, S., Kretzschmar, H., (2001) J. Biol. Chem, 276, pp. 16711-16719
Bonomo, R.P., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., Tabbi, G., (2000) Chem. Eur. J, 6, pp. 4195-4202
Bonomo, R.P., Cucinotta, V., Giuffrida, A., Impellizzeri, G., Magrì, A., Pappalardo, G., Rizzarelli, E., Vagliasindi, L.I., (2005) Dalton Trans, pp. 150-158
Morante, S., Gonzalez-Iglesias, R., Potrich, C., Meneghini, C., Meyer-Klaucke, W., Menestrina, G., Gasset, M., (2004) J. Biol. Chem, 279, pp. 11753-11759
Valensin, D., Luczkowski, M., Mancini, F.M., Legowska, A., Gaggelli, E., Valensin, G., Rolka, K., Kozlowski, H., (2004) Dalton Trans, pp. 1284-1293
Chattopadhyay, M., Walter, E.D., Newell, D.J., Jackson, P.J., Aronoff-Spencer, E., Peisach, J., Gerfen, G.J., Millhauser, G.L., (2005) J. Am. Chem. Soc, 127, pp. 12647-12656
Jones, C.E., Abdelraheim, S.R., Brown, D.R., Viles, J.H., (2004) J. Biol. Chem, 279, pp. 32018-32027
Jones, C.E., Klewpatinond, M., Abdelraheim, S.R., Brown, D.R., Viles, J.H., (2005) J. Mol. Biol, 346, pp. 1393-1407
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
Thompsett, A.R., Abdelraheim, S.R., Daniels, M., Brown, D.R., (2005) J. Biol. Chem, 280, pp. 42750-42758
Jobling, M.F., Huang, X., Stewart, L.R., Barnham, K.J., Curtain, C., Volitakis, I., Perugini, M., Cappai, R., (2001) Biochemistry, 40, pp. 8073-8084
Belosi, B., Gaggelli, E., Guerrini, R., Kozlowski, H., Luczkowski, M., Mancini, F.M., Remelli, M., Valensin, G., (2004) ChemBioChem, 5, pp. 349-359
Jószai, V., Nagy, Z., Osz, K., Sanna, D., Di Natale, G., La Mendola, D., Pappalardo, G., Sóvágó, I., (2006) J. Inorg. Biochem, 100, pp. 1399-1409
Grasso, D., Grasso, G., Guantieri, V., Impellizzeri, G., La Rosa, C., Milardi, D., Micera, G., Sóvágó, I., (2006) Chem. Eur J, 12, pp. 537-547
Gans, P., Sabatini, A., Vacca, A., (1996) Talanta, 43, pp. 1739-1753
Gaggelli, E., Kozlowski, H., Valensin, D., Valensin, G., (2006) Chem. Rev, 106, pp. 1995-2044
Luczkowski, M., Kozlowski, H., Stawikowski, M., Rolka, K., Gaggelli, E., Valensin, D., Valensin, G., (2002) J. Chem. Soc. Dalton Trans, pp. 2269-2274
Brown, D.R., Kozlowski, H., (2004) Dalton Trans, pp. 1907-1917
Kozlowski, H., Bal, W., Dyba, M., Kowalik-Jankowska, T., (1999) Coord. Chem. Rev, 184, pp. 319-346
Sanna, D., Micera, G., Kállay, C., Rigó, V., Sóvágó, I., (2004) Dalton Trans, pp. 2702-2707
Kállay, C., Várnagy, K., Malandrinos, G., Hadjiliadis, N., Sanna, D., Sóvágó, I., (2006) Dalton Trans, pp. 4545-4552
Casolaro, M., Chelli, M., Ginanneschi, M., Laschi, F., Messori, L., Muniz-Miranda, M., Papini, A.M., Kozlowski, H., (2002) J. Inorg. Biochem, 89, pp. 181-190
Brasun, J., Gabbiani, C., Ginanneschi, M., Messori, L., Orfei, M., Swiatek-Kozlowska, J., (2004) J. Inorg. Biochem, 98, pp. 2016-2021
Bóka, B., Myari, A., Sóvágó, I., Hadjiliadis, N., (2004) J. Inorg. Biochem, 98, pp. 113-122
Luczkowski, M., Wisniewska, K., Lankiewicz, L., Kozlowski, H., (2002) J. Chem. Soc. Dalton Trans, pp. 2266-2268
Remelli, M., Luczkowski, M., Bonna, A.M., Mackiewicz, Z., Conato, C., Kozlowski, H., (2003) New J. Chem, 27, pp. 245-250
Bonomo, R.R., Casella, L., De Gioia, L., Molinari, H., Impellizzeri, G., Jordan, T., Pappalardo, G., Rizzarelli, E., (1997) J. Chem. Soc. Dalton Trans, pp. 2387-2389
Pappalardo, G., Impellizzeri, G., Bonomo, R.P., Campagna, T., Grasso, G., Saita, M.G., (2002) New J. Chem, 26, pp. 593-600
Jancsó, A., Paksi, Z., Jakab, N., Gyurcsik, B., Rockenbauer, A., Gajda, T., (2005) Dalton Trans, pp. 3187-3194
Zékány, L., Nagypál, I., (1985) Computational Methods for the Determination of Stability Constants, pp. 291-355. , Ed.:D. J. Leggett, Plenum, New York
Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details
A 31-mer polypeptide, which encompasses residues 84-114 of human prion protein HuPrP(84-114) and contains three histidyl residues, namely one from the octarepeat (His85) and two histidyl residues from outside the octarepeat region (His96 and His111), and its mutants with two histidyl residues HuPrP(84-114)His85Ala, HuPrP(84-114) His96Ala, HuPrP(84-114)His111Ala and HuPrP(91-115) have been synthesised and their Cu2+ complexes studied by potentiometric and spectroscopic (UV/Vis, CD, EPR, ESI-MS) techniques. The results revealed a high Cu2+-binding affinity of all peptides, and the spectroscopic studies made it possible to clarify the coordination mode of the peptides in the different complex species. The imidazole nitrogen donor atoms of histidyl residues are the exclusive metal-binding sites below pH 5.5, and they have a preference for macrochelate structure formation. The deprotonation and metal-ion coordination of amide functions take place by increasing the pH; all of the histidines can be considered to be independent metal-binding sites in these species. As a consequence, di- and trinuclear complexes can be present even in equimolar samples of the metal ion and peptides, but the ratios of polynuclear species do not exceed the statistically expected ones; this excludes the possibility of cooperative Cu2+ binding. The species with a (N(im),N,N)-binding mode are favoured around pH 7, and their stability is enhanced by the macrochelation from another histidyl residue in the mononuclear complexes. The independence of the histidyl sites results in the existence of coordination isomers and the preference for metal binding follows the order of: His111>His96>His85. Deprotonation and metal-ion coordination of the third amide functions were detected in slightly alkaline solutions at each of the metal-binding sites; all had a (N(im),N,N,N)-coordination mode. Spectroscopic measurements also made it clear that the four lysyl amino groups of the peptides are not metal-binding sites in any cases.
Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details
Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details
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(387 visite) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
711 Records (682 escludendo Abstract e Conferenze). Impact factor totale: 2532.943 (2454.183 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 2630.84 (2544.446 escludendo Abstract e Conferenze).
Last modified by Ultima modifica di Marco Comerci on in data Sunday 12 July 2020, 13:15:05 353 views visite. Last view on Ultima visita in data Friday 26 February 2021, 3:36:08