A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1135 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.476, 5-year impact factor: 5.477
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952728882&partnerID=40&md5=bfa042f2e7a6f2bdbe61b2849a22f99d
Keywords: Copper, Doppel Proteins, Helical Structures, Peptides, Prions, Amino Acid Residues, Aqueous Solutions, Asparagine Residue, Aspartates, Carboxylate Groups, Cd Measurements, Cd Spectra, Coordination Environment, Copper Complexes, Copper Ions, Epr Parameters, Helical Conformation, Helix Peptide, Histidine Residues, Loop Regions, Metal Binding, Metal-Binding Sites, N-Terminal Domains, Neurotoxicity, Peptide Conformation, Peptide Fragments, Physiological Ph Range, Potentiometric Titrations, Prion Protein, Protein Domains, Protein Functions, Secondary Structures, Spectroscopic Measurements, Spectroscopic Parameters, Spectroscopic Studies, Stability Constants, Transgenic Mice, Uv Region, Binding Energy, Biochemistry, Carboxylation, Complexation, Coordination Reactions, Data Storage Equipment, Electron Spin Resonance Spectroscopy, Metal Complexes, Metal Ions, Organic Acids, Ph Effects, Phosphatases, Plants (botany), Spectroscopic Analysis, Synthesis (chemical), Copper Compounds, Glycosylphosphatidylinositol Anchored Protein, Prnd Protein, Human, Amino Acid Sequence, Article, Circular Dichroism, Protein Binding, Protein Secondary Structure, Thermodynamics, Ultraviolet Spectrophotometry, Gpi-Linked Proteins, Protein Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy
Istituto di Biostrutlure e Bioimmagini, CNR, c/o Dipartimento di Scienze Chimiche Viale A. Doria 6, 95125 Catania, Italy
Department of Chemistry, University of Gothenburg, PO Box 462, SE-405 30 Gothenburg, Sweden
Istituto Nazionale di Biostrutture e Biosistemi, Consorzio Interuniversitario, Viale Medaglie d'oro 305, 00136 Roma, Italy
Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, H3C 3J7, Canada
D partement de Biochimie, Universit de Montr al, C. P. 6128 Succursale Centre-Ville, Montr al, QC, H3C 3J7, Canada
References:
Peoc'H, K., Serres, C., Erobert, Y., Martin, C., Lehmann, S., Chasseigneaux, S., Sazdovitch, V., Laplanche, J.L., (2002) J Biol. Chem., 277, pp. 43071-4307
Li, A., Sakaguchi, S., Shigematsu, K., Atarashi, R., Roy, B.C., Nakaoke, R., Arima, K., Katamine, S., (2000) Am, J. Pathol., 157, pp. 1447-1452
Behrens, A., Genoud, N., Naumann, H., Rulicke, T., Janett, F., Heppner, F.L., Ledermann, B., Aguzzi, A., (2002) EMBO J., 21, pp. 3652-3658
Sakaguchi, S., Katamine, S., Nishida, N., Moriuchi, R., Shigematsu, K., Sugimoto, T., Nakatani, A., Noda, T., (1996) Nature, 380, pp. 528-531
Moore, C., Lee, I.Y., Silverman, G.L., Harrison, P.M., Strome, R., Heinrich, C., Karunaratne, A., Westaway, D., (1999) J. Mol. Biol., 292, pp. 797-817
Shaked, Y., Rosenmann, H., Talmor, G., Gabizon, R., (1999) J. Biol. Chem., 274, pp. 32153-32158
Lührs, T., Riek, R., Giert, P., Wutrich, K., (2003) J. Mol. Biol., 326, pp. 1549-1557
Rossi, D., Cozzio, A., Flechsig, E., Klein, M.A., Rulicke, T., Aguzzi, A., Weissmann, C., (2001) EMBO J., 20, pp. 694-702
Anderson, L., Rossi, D., Linehan, J., Brandner, S., Weissmann, C., (2004) Proc. Natl. Acad. Sci. USA, 101, pp. 3644-3649
Radovanovic, I., Braun, N., Giger, O.T., Mertz, K., Miele, G., Prinz, M., Navarro, B., Aguzzi, A., (2005) J. Neurosci., 25, pp. 4879-4888
Mo, H., Moore, R.C., Cohen, F.E., Westaway, D., Prusiner, S.B., Wright, P.E., Dyson, H.J., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 2352-2357
Watts, J.C., Westaway, D., (2007) Biochim. Biophys. Acta Mol. Basis Dis., 1772, pp. 654-672
Qin, K., O'Donnel, M., Zhao, R.Y., (2006) Neuroscience, 141, pp. 1-8
Yoshikawa, D., Yamaguchi, N., Ishibashi, D., Yamanaka, H., Okimura, N., Yamaguchi, Y., Mori, T., Sakaguchi, S., (2008) J. Biol. Chem., 283, pp. 24202-24211
Behrens, A., (2003) Br. Med. Bull., 66, pp. 35-42
Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., Stromer, R., Fraser, P.E., Kretzschmar, H., (1997) Nature, 390, pp. 662-687
Millhauser, G.L., (2007) Ann. Pharm. Belg., 58, pp. 299-320
Bonomo, R.P., La Mendola, D., Pappalardo, G., Rizzarelli, E., Sovago, I., (2006) Recent Development in Bioinorganic Chemistry: Metal Complexes of Bioactive Molecules, pp. 133-160. , Ed.: M. Saviano Transworld Research Network, Kerala
Qin, K., Coomaraswamy, J., Mastrangelo, P., Yang, Y., Lugowski, S., Petromilli, C., Prusiner, S.B., Westaway, D., (2003) J. Biol. Chem, 278, pp. 8888-8896
Cereghetti, G.M., Negro, A., Massimino, M.L., Sorgato, M.C., Van Doorslaer, S., (2004) J. Biol. Chem., 279, pp. 36497-36503
Drisaldi, B., Coomaraswamy, J., Mastrangelo, P., Strome, B., Yang, J., Watts, J.C., Chishti, M.A., Westaway, D., (2004) J. Biol. Chem., 279, pp. 55443-55454
La Mendola, D., Magrì, A., Hansson, Ö., Bonomo, R.P., Rizzarelli, E., (2009) J. Inorg. Biochem., 103, pp. 758-765
Nicoll, A.J., Milelr, D.J., Futterer, K., Ravelli, R., Allemann, R.K., (2006) J. Am. Chem. Soc., 128, pp. 9187-9193
Böhm, G., Muhr, R., Jaenicke, R., (1992) Protein Eng., 5, pp. 191-195
Chakrabartty, A., Kortemme, T., Padmanabhan, S., Baldwin, R.L., (1993) Biochemistry, 32, pp. 5560-5565
Woody, R.W., Dunker, A.K., (1996) Circular Dichroism and the Conformational Analysis of Biomolecules, pp. 109-157. , Ed.: GD. Fasman Plenum Press, New York
Kállay, C., Varnagy, K., Micera, G., Sanna, D., Sovago, I., (2005) J. Inorg. Biochem., 99, pp. 1514-1525
Bóka, B., Myari, A., Sovago, I., Hadjiliadis, N., (2004) J. Inorg Biochem., 95, pp. 113-122
La Mendola, D., Bonomo, R.P., Impellizzeri, G., Maccarrone, G., Pappalardo, G., Rizzarelli, E., Pietropaolo, A., Zito, V., (2005) J. Biol. Inorg. Chem., 10, pp. 463-475
Guangshun, W., Peterkofsky, A., Keifer, P.A., Li, X., (2005) Protein Sci., 14, pp. 1082-1090
Osz, K., Sovago, I., (2006) Dalton Trans., pp. 3841-3854
Benvegnù, S., Franciotta, D., Sussman, J., Bachi, A., Cardini, E., Torreri, P., Govaerts, C., Legname, G., (2009) PLos One., 4, pp. e5968
Li, P., Dong, C., Lei, Y., Shan, B., Xiao, X., Jiang, H., Wang, X., Dong, X., (2009) Acta Biochim. Biophys. Sin., 47, pp. 42-53
Bonomo, R.P., Cucinotta, V., Giuffrida, A., Impellizzeri, G., Magrì, A., Pappalardo, G., Rizzarelli, E., Vagliasindi, L.I., (2005) Dalton Trans., pp. 150-158
Valensin, D., Luczkowski, M., Mancini, F.M., Legowska, A., Gaggelli, E., Valensin, G., Rolka, K., Kozlowski, H., (2004) Dalton Trans., pp. 1284-1293
Cereghetti, G.M., Schweiger, A., Glockshuber, R., Van Doorslaer, S., (2001) Biophys. J., 81, pp. 516-525
Brown, D.R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., (2004) J. Inorg. Biochem., 98, pp. 133-143
Grasso, D., Grasso, G., Guantieri, V., Impellizzeri, G., La Rosa, C., Milardi, D., Micera, G., Sovago, I., (2006) Chem. Eur. J., 12, pp. 537-547
Bonomo, R.P., Calì, R., Cucinotta, V., Impellizzeri, G., Rizzarelli, E., (1986) Inorg. Chem., 25, pp. 1641-1646
Gans, P., Sabatini, A., Vacca, A., (1996) Talanta, 43, pp. 1739-1753
Alderighi, L., Gans, P., Lenco, A., Peters, D., Sabatini, A., Vacca, A., (1999) Coord. Chem. Rev., 184, pp. 311-318
Bartels, C., Xia, T., Billeter, M., Güntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, pp. 1-10
Rance, M., Sørensen, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R., Wüthrich, K., (1983) Biochem. Biophys. Res. Commun., 117, pp. 479-485
Braunschweiler, L., Ernst, R.R., (1983) J. Magn. Resort., 53, pp. 521-528
Griesinger, C., Ernst, R.R., (1987) J. Magn. Reson., 75, pp. 261-271
Kumar, A., Ernst, R.R., Wüthrich, K., (1980) Biochem. Biophys. Res. Commun., 95, pp. 1-6
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Stejskal, E.O., Tanner, J.E., (1965) J. Chem. Phys., 42, pp. 288-292
Chatterjee, C., Majumder, B., Mukhopadhyay, C., (2004) J. Phys. Chem. B, 108, pp. 7430-7436
Herrmann, T., Güntert, P., Wüthrich, K., (2002) J. Mol. Biol., 319, pp. 209-227
Gunsteren, W.F., Billeter, S.R., Eising, A.A., Hünenberger, P.H., Krüger, P., Mark, A.E., Scott, W.R.P., Tironi, I.G., (1996) Biomolecular Simulation: The GROMOS96 Manual and User Guide (BIOMOs)
Guex, N., Peitsch, M.C., (1997) Electrophoresis, 18, pp. 2714-2723
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graph., 14, pp. 51-55
Moore, C., Lee, I. Y., Silverman, G. L., Harrison, P. M., Strome, R., Heinrich, C., Karunaratne, A., Westaway, D., (1999) J. Mol. Biol., 292, pp. 797-817
L hrs, T., Riek, R., Giert, P., Wutrich, K., (2003) J. Mol. Biol., 326, pp. 1549-1557
Mo, H., Moore, R. C., Cohen, F. E., Westaway, D., Prusiner, S. B., Wright, P. E., Dyson, H. J., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 2352-2357
Watts, J. C., Westaway, D., (2007) Biochim. Biophys. Acta Mol. Basis Dis., 1772, pp. 654-672
Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Stromer, R., Fraser, P. E., Kretzschmar, H., (1997) Nature, 390, pp. 662-687
Millhauser, G. L., (2007) Ann. Pharm. Belg., 58, pp. 299-320
Bonomo, R. P., La Mendola, D., Pappalardo, G., Rizzarelli, E., Sovago, I., (2006) Recent Development in Bioinorganic Chemistry: Metal Complexes of Bioactive Molecules, pp. 133-160. , Ed.: M. Saviano Transworld Research Network, Kerala
Cereghetti, G. M., Negro, A., Massimino, M. L., Sorgato, M. C., Van Doorslaer, S., (2004) J. Biol. Chem., 279, pp. 36497-36503
Nicoll, A. J., Milelr, D. J., Futterer, K., Ravelli, R., Allemann, R. K., (2006) J. Am. Chem. Soc., 128, pp. 9187-9193
B hm, G., Muhr, R., Jaenicke, R., (1992) Protein Eng., 5, pp. 191-195
Woody, R. W., Dunker, A. K., (1996) Circular Dichroism and the Conformational Analysis of Biomolecules, pp. 109-157. , Ed.: GD. Fasman Plenum Press, New York
K llay, C., Varnagy, K., Micera, G., Sanna, D., Sovago, I., (2005) J. Inorg. Biochem., 99, pp. 1514-1525
B ka, B., Myari, A., Sovago, I., Hadjiliadis, N., (2004) J. Inorg Biochem., 95, pp. 113-122
Benvegn, S., Franciotta, D., Sussman, J., Bachi, A., Cardini, E., Torreri, P., Govaerts, C., Legname, G., (2009) PLos One., 4, pp. e5968
Bonomo, R. P., Cucinotta, V., Giuffrida, A., Impellizzeri, G., Magr, A., Pappalardo, G., Rizzarelli, E., Vagliasindi, L. I., (2005) Dalton Trans., pp. 150-158
Brown, D. R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., (2004) J. Inorg. Biochem., 98, pp. 133-143
Bonomo, R. P., Cal, R., Cucinotta, V., Impellizzeri, G., Rizzarelli, E., (1986) Inorg. Chem., 25, pp. 1641-1646
Rance, M., S rensen, O. W., Bodenhausen, G., Wagner, G., Ernst, R. R., W thrich, K., (1983) Biochem. Biophys. Res. Commun., 117, pp. 479-485
Hwang, T. L., Shaka, A. J., (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Stejskal, E. O., Tanner, J. E., (1965) J. Chem. Phys., 42, pp. 288-292
Herrmann, T., G ntert, P., W thrich, K., (2002) J. Mol. Biol., 319, pp. 209-227
Gunsteren, W. F., Billeter, S. R., Eising, A. A., H nenberger, P. H., Kr ger, P., Mark, A. E., Scott, W. R. P., Tironi, I. G., (1996) Biomolecular Simulation: The GROMOS96 Manual and User Guide (BIOMOs)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.476, 5-year impact factor: 5.477
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952728882&partnerID=40&md5=bfa042f2e7a6f2bdbe61b2849a22f99d
Keywords: Copper, Doppel Proteins, Helical Structures, Peptides, Prions, Amino Acid Residues, Aqueous Solutions, Asparagine Residue, Aspartates, Carboxylate Groups, Cd Measurements, Cd Spectra, Coordination Environment, Copper Complexes, Copper Ions, Epr Parameters, Helical Conformation, Helix Peptide, Histidine Residues, Loop Regions, Metal Binding, Metal-Binding Sites, N-Terminal Domains, Neurotoxicity, Peptide Conformation, Peptide Fragments, Physiological Ph Range, Potentiometric Titrations, Prion Protein, Protein Domains, Protein Functions, Secondary Structures, Spectroscopic Measurements, Spectroscopic Parameters, Spectroscopic Studies, Stability Constants, Transgenic Mice, Uv Region, Binding Energy, Biochemistry, Carboxylation, Complexation, Coordination Reactions, Data Storage Equipment, Electron Spin Resonance Spectroscopy, Metal Complexes, Metal Ions, Organic Acids, Ph Effects, Phosphatases, Plants (botany), Spectroscopic Analysis, Synthesis (chemical), Copper Compounds, Glycosylphosphatidylinositol Anchored Protein, Prnd Protein, Human, Amino Acid Sequence, Article, Circular Dichroism, Protein Binding, Protein Secondary Structure, Thermodynamics, Ultraviolet Spectrophotometry, Gpi-Linked Proteins, Protein Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università Degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy
Istituto di Biostrutlure e Bioimmagini, CNR, c/o Dipartimento di Scienze Chimiche Viale A. Doria 6, 95125 Catania, Italy
Department of Chemistry, University of Gothenburg, PO Box 462, SE-405 30 Gothenburg, Sweden
Istituto Nazionale di Biostrutture e Biosistemi, Consorzio Interuniversitario, Viale Medaglie d'oro 305, 00136 Roma, Italy
Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC, H3C 3J7, Canada
D partement de Biochimie, Universit de Montr al, C. P. 6128 Succursale Centre-Ville, Montr al, QC, H3C 3J7, Canada
References:
Peoc'H, K., Serres, C., Erobert, Y., Martin, C., Lehmann, S., Chasseigneaux, S., Sazdovitch, V., Laplanche, J.L., (2002) J Biol. Chem., 277, pp. 43071-4307
Li, A., Sakaguchi, S., Shigematsu, K., Atarashi, R., Roy, B.C., Nakaoke, R., Arima, K., Katamine, S., (2000) Am, J. Pathol., 157, pp. 1447-1452
Behrens, A., Genoud, N., Naumann, H., Rulicke, T., Janett, F., Heppner, F.L., Ledermann, B., Aguzzi, A., (2002) EMBO J., 21, pp. 3652-3658
Sakaguchi, S., Katamine, S., Nishida, N., Moriuchi, R., Shigematsu, K., Sugimoto, T., Nakatani, A., Noda, T., (1996) Nature, 380, pp. 528-531
Moore, C., Lee, I.Y., Silverman, G.L., Harrison, P.M., Strome, R., Heinrich, C., Karunaratne, A., Westaway, D., (1999) J. Mol. Biol., 292, pp. 797-817
Shaked, Y., Rosenmann, H., Talmor, G., Gabizon, R., (1999) J. Biol. Chem., 274, pp. 32153-32158
Lührs, T., Riek, R., Giert, P., Wutrich, K., (2003) J. Mol. Biol., 326, pp. 1549-1557
Rossi, D., Cozzio, A., Flechsig, E., Klein, M.A., Rulicke, T., Aguzzi, A., Weissmann, C., (2001) EMBO J., 20, pp. 694-702
Anderson, L., Rossi, D., Linehan, J., Brandner, S., Weissmann, C., (2004) Proc. Natl. Acad. Sci. USA, 101, pp. 3644-3649
Radovanovic, I., Braun, N., Giger, O.T., Mertz, K., Miele, G., Prinz, M., Navarro, B., Aguzzi, A., (2005) J. Neurosci., 25, pp. 4879-4888
Mo, H., Moore, R.C., Cohen, F.E., Westaway, D., Prusiner, S.B., Wright, P.E., Dyson, H.J., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 2352-2357
Watts, J.C., Westaway, D., (2007) Biochim. Biophys. Acta Mol. Basis Dis., 1772, pp. 654-672
Qin, K., O'Donnel, M., Zhao, R.Y., (2006) Neuroscience, 141, pp. 1-8
Yoshikawa, D., Yamaguchi, N., Ishibashi, D., Yamanaka, H., Okimura, N., Yamaguchi, Y., Mori, T., Sakaguchi, S., (2008) J. Biol. Chem., 283, pp. 24202-24211
Behrens, A., (2003) Br. Med. Bull., 66, pp. 35-42
Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., Stromer, R., Fraser, P.E., Kretzschmar, H., (1997) Nature, 390, pp. 662-687
Millhauser, G.L., (2007) Ann. Pharm. Belg., 58, pp. 299-320
Bonomo, R.P., La Mendola, D., Pappalardo, G., Rizzarelli, E., Sovago, I., (2006) Recent Development in Bioinorganic Chemistry: Metal Complexes of Bioactive Molecules, pp. 133-160. , Ed.: M. Saviano Transworld Research Network, Kerala
Qin, K., Coomaraswamy, J., Mastrangelo, P., Yang, Y., Lugowski, S., Petromilli, C., Prusiner, S.B., Westaway, D., (2003) J. Biol. Chem, 278, pp. 8888-8896
Cereghetti, G.M., Negro, A., Massimino, M.L., Sorgato, M.C., Van Doorslaer, S., (2004) J. Biol. Chem., 279, pp. 36497-36503
Drisaldi, B., Coomaraswamy, J., Mastrangelo, P., Strome, B., Yang, J., Watts, J.C., Chishti, M.A., Westaway, D., (2004) J. Biol. Chem., 279, pp. 55443-55454
La Mendola, D., Magrì, A., Hansson, Ö., Bonomo, R.P., Rizzarelli, E., (2009) J. Inorg. Biochem., 103, pp. 758-765
Nicoll, A.J., Milelr, D.J., Futterer, K., Ravelli, R., Allemann, R.K., (2006) J. Am. Chem. Soc., 128, pp. 9187-9193
Böhm, G., Muhr, R., Jaenicke, R., (1992) Protein Eng., 5, pp. 191-195
Chakrabartty, A., Kortemme, T., Padmanabhan, S., Baldwin, R.L., (1993) Biochemistry, 32, pp. 5560-5565
Woody, R.W., Dunker, A.K., (1996) Circular Dichroism and the Conformational Analysis of Biomolecules, pp. 109-157. , Ed.: GD. Fasman Plenum Press, New York
Kállay, C., Varnagy, K., Micera, G., Sanna, D., Sovago, I., (2005) J. Inorg. Biochem., 99, pp. 1514-1525
Bóka, B., Myari, A., Sovago, I., Hadjiliadis, N., (2004) J. Inorg Biochem., 95, pp. 113-122
La Mendola, D., Bonomo, R.P., Impellizzeri, G., Maccarrone, G., Pappalardo, G., Rizzarelli, E., Pietropaolo, A., Zito, V., (2005) J. Biol. Inorg. Chem., 10, pp. 463-475
Guangshun, W., Peterkofsky, A., Keifer, P.A., Li, X., (2005) Protein Sci., 14, pp. 1082-1090
Osz, K., Sovago, I., (2006) Dalton Trans., pp. 3841-3854
Benvegnù, S., Franciotta, D., Sussman, J., Bachi, A., Cardini, E., Torreri, P., Govaerts, C., Legname, G., (2009) PLos One., 4, pp. e5968
Li, P., Dong, C., Lei, Y., Shan, B., Xiao, X., Jiang, H., Wang, X., Dong, X., (2009) Acta Biochim. Biophys. Sin., 47, pp. 42-53
Bonomo, R.P., Cucinotta, V., Giuffrida, A., Impellizzeri, G., Magrì, A., Pappalardo, G., Rizzarelli, E., Vagliasindi, L.I., (2005) Dalton Trans., pp. 150-158
Valensin, D., Luczkowski, M., Mancini, F.M., Legowska, A., Gaggelli, E., Valensin, G., Rolka, K., Kozlowski, H., (2004) Dalton Trans., pp. 1284-1293
Cereghetti, G.M., Schweiger, A., Glockshuber, R., Van Doorslaer, S., (2001) Biophys. J., 81, pp. 516-525
Brown, D.R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., (2004) J. Inorg. Biochem., 98, pp. 133-143
Grasso, D., Grasso, G., Guantieri, V., Impellizzeri, G., La Rosa, C., Milardi, D., Micera, G., Sovago, I., (2006) Chem. Eur. J., 12, pp. 537-547
Bonomo, R.P., Calì, R., Cucinotta, V., Impellizzeri, G., Rizzarelli, E., (1986) Inorg. Chem., 25, pp. 1641-1646
Gans, P., Sabatini, A., Vacca, A., (1996) Talanta, 43, pp. 1739-1753
Alderighi, L., Gans, P., Lenco, A., Peters, D., Sabatini, A., Vacca, A., (1999) Coord. Chem. Rev., 184, pp. 311-318
Bartels, C., Xia, T., Billeter, M., Güntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, pp. 1-10
Rance, M., Sørensen, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R., Wüthrich, K., (1983) Biochem. Biophys. Res. Commun., 117, pp. 479-485
Braunschweiler, L., Ernst, R.R., (1983) J. Magn. Resort., 53, pp. 521-528
Griesinger, C., Ernst, R.R., (1987) J. Magn. Reson., 75, pp. 261-271
Kumar, A., Ernst, R.R., Wüthrich, K., (1980) Biochem. Biophys. Res. Commun., 95, pp. 1-6
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Stejskal, E.O., Tanner, J.E., (1965) J. Chem. Phys., 42, pp. 288-292
Chatterjee, C., Majumder, B., Mukhopadhyay, C., (2004) J. Phys. Chem. B, 108, pp. 7430-7436
Herrmann, T., Güntert, P., Wüthrich, K., (2002) J. Mol. Biol., 319, pp. 209-227
Gunsteren, W.F., Billeter, S.R., Eising, A.A., Hünenberger, P.H., Krüger, P., Mark, A.E., Scott, W.R.P., Tironi, I.G., (1996) Biomolecular Simulation: The GROMOS96 Manual and User Guide (BIOMOs)
Guex, N., Peitsch, M.C., (1997) Electrophoresis, 18, pp. 2714-2723
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graph., 14, pp. 51-55
Moore, C., Lee, I. Y., Silverman, G. L., Harrison, P. M., Strome, R., Heinrich, C., Karunaratne, A., Westaway, D., (1999) J. Mol. Biol., 292, pp. 797-817
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A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein
The doppel protein (Dpi) is the first homologue of the prion protein (PrP C) to be discovered; it is overexpressed in transgenic mice that lack the prion gene, resulting in neurotoxicity. The whole prion protein is able to inhibit Dpi neurotoxicity, and its N-terminal domain is the determinant part of the protein function. This region represents the main copper(II) binding site of PrP C. Dpi is able to bind at least one copper ion, and the specific metalbinding site has been identified as the histidine residue at the beginning of the third helical region. However, a reliable characterization of copper(II) coordination features has not been reported. In a previous paper, we studied the copper(II) interaction with a peptide that encompasses only the loop region potentially involved in metal binding. Nevertheless, we did not find a complete match between the EPR spectroscopic parameters of the copper(II) complexes formed with the synthesized peptide and those reported for the copper(II) binding sites of the whole protein. Herein, the synthesis of the human Dpi peptide fragment hDpl(122-139) (Ac-KPDNKLHQQVLWRLVQEL-NH 2) and its copper(II) complex species are reported. This peptide encompasses the third a helix and part of the loop linking the second and the third helix of human doppel protein. The single-point-mutated peptide, hDpl(122-139)D124N, in which aspartate 124 replaces an asparagine residue, was also synthesized. This peptide was used to highlight the role of the carboxylate group on both the conformation preference of the Dpi fragment and its copper(II) coordination features. NMR spectroscopic measurements show that the hDpl( 122-139) peptide fragment is in the prevailing ahelix conformation. It is localized within the 127-137 amino acid residue region that represents a reliable conformational mimic of the related protein domain. A comparison with the singlepoint-mutated hDpl(122-139)D124N reveals the significant role played by the aspartic residue in addressing the peptide conformation towards a helical structure. It is further confirmed by CD measurements. Potentiometric titrations were carried out in aqueous solutions to obtain the stability constant values of the species formed by copper(II) with the hDpl peptides. Spectroscopic studies (EPR, NMR, CD, UV/Vis) were performed to characterize the coordination environments of the different metal complexes. The EPR parameters of the copper(II) complexes with hDpl( 122-139) match those of the previously reported copper(II) binding sites of the whole hDpl. Addition of the copper(II) ion to the peptide fragment does not alter the helical conformation of hDpl(122-139), as shown by CD spectra in the far-UV region. The aspartate-driven preorganized secondary structure is not significantly modified by the involvement of Aspl24 in the copper(II) complex species that form in the physiological pH range. To elaborate on the potential role of copper(II) in the recently reported interaction between the PrP C and Dpi, the affinity of the copper(II) complexes towards the prion N terminus domain and the binding site of Dpi was reported. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
The doppel protein (Dpi) is the first homologue of the prion protein (PrP C) to be discovered; it is overexpressed in transgenic mice that lack the prion gene, resulting in neurotoxicity. The whole prion protein is able to inhibit Dpi neurotoxicity, and its N-terminal domain is the determinant part of the protein function. This region represents the main copper(II) binding site of PrP C. Dpi is able to bind at least one copper ion, and the specific metalbinding site has been identified as the histidine residue at the beginning of the third helical region. However, a reliable characterization of copper(II) coordination features has not been reported. In a previous paper, we studied the copper(II) interaction with a peptide that encompasses only the loop region potentially involved in metal binding. Nevertheless, we did not find a complete match between the EPR spectroscopic parameters of the copper(II) complexes formed with the synthesized peptide and those reported for the copper(II) binding sites of the whole protein. Herein, the synthesis of the human Dpi peptide fragment hDpl(122-139) (Ac-KPDNKLHQQVLWRLVQEL-NH 2) and its copper(II) complex species are reported. This peptide encompasses the third a helix and part of the loop linking the second and the third helix of human doppel protein. The single-point-mutated peptide, hDpl(122-139)D124N, in which aspartate 124 replaces an asparagine residue, was also synthesized. This peptide was used to highlight the role of the carboxylate group on both the conformation preference of the Dpi fragment and its copper(II) coordination features. NMR spectroscopic measurements show that the hDpl( 122-139) peptide fragment is in the prevailing ahelix conformation. It is localized within the 127-137 amino acid residue region that represents a reliable conformational mimic of the related protein domain. A comparison with the singlepoint-mutated hDpl(122-139)D124N reveals the significant role played by the aspartic residue in addressing the peptide conformation towards a helical structure. It is further confirmed by CD measurements. Potentiometric titrations were carried out in aqueous solutions to obtain the stability constant values of the species formed by copper(II) with the hDpl peptides. Spectroscopic studies (EPR, NMR, CD, UV/Vis) were performed to characterize the coordination environments of the different metal complexes. The EPR parameters of the copper(II) complexes with hDpl( 122-139) match those of the previously reported copper(II) binding sites of the whole hDpl. Addition of the copper(II) ion to the peptide fragment does not alter the helical conformation of hDpl(122-139), as shown by CD spectra in the far-UV region. The aspartate-driven preorganized secondary structure is not significantly modified by the involvement of Aspl24 in the copper(II) complex species that form in the physiological pH range. To elaborate on the potential role of copper(II) in the recently reported interaction between the PrP C and Dpi, the affinity of the copper(II) complexes towards the prion N terminus domain and the binding site of Dpi was reported. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein
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A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein
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Mercurio FA, Di Natale C, Pirone L, Vincenzi M, Marasco D, De Luca S, Pedone EM, Leone M
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Chino M, Maglio O, Nastri F, Pavone V, Degrado WF, Lombardi A
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Tabbì G, Di Mauro G, Purrello R, Bonomo RP
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Vagliasindi LI, Arena G, Bonomo RP, Pappalardo G, Tabbì G
* Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein (357 views)
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Impact Factor: 3.838
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Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
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Banyasz A, Karpati S, Mercier Y, Reguero M, Gustavsson T, Markovitsi D, Improta R
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Alterio V, Monti SM, Truppo E, Pedone C, Supuran CT, De Simone G
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Mazzaglia A, Micali N, Scolaro LM, Attanasio F, Magrí A, Pappalardo G, Villari V
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Improta R, Santoro F, Barone V, Lami A
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Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
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Improta R, Barone V, Lami A, Santoro F
* Quantum dynamics of the ultrafast ππ*/nπ* population transfer in uracil and 5-fluoro-uracil in water and acetonitrile (289 views)
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Marasco D, Stilo R, Sandomenico A, Monti SM, Tizzano B, De Capua A, Varricchio E, Liguoro D, Zotti T, Formisano S, Ruvo M, Vito P
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Karunakaran V, Kleinermanns K, Improta R, Kovalenko SA
* Photoinduced dynamics of guanosine monophosphate in water from broad-band transient absorption spectroscopy and quantum-chemical calculations (278 views)
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Sgarlata C, Bonaccorso C, Gulino FG, Zito V, Arena G, Sciotto D
* Sterochemistry And Thermodynamics Of The Inclusion Of Aliphatic And Aromatic Anionic Guests In A Tetracationic Calix [4] Arene In Acidic And Neutral Aqueous Solutions (311 views)
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Santoro F, Barone V, Improta R
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Diana D, Ziaco B, Colombo G, Scarabelli G, Romanelli A, Fedone C, Fattorusso R, D'Andrea LD
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Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
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Zubrzak P, Banas A, Kaczmarek K, Leplawy MT, Sochacki M, Kowalski ML, Szkudlinska B, Zabrocki J, Di Lello P, Isernia C, Saviano M, Pedone C, Benedetti E
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Saviano M, Improta R, Benedetti E, Carrozzini B, Cascarano GL, Didierjean C, Toniolo C, Crisma M
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Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
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Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
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Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
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Benedetti E, Iacovino R, Pedone C, Rossi F, Saviano M, Isernia C, Montesarchio D, DeNapoli L, Piccialli G
β-Amino acid residues: Conformational characterization of an N- and C-protected homo-β-(S)-leucine (314 views)
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Nastri F, Lombardi A, Morelli G, Maglio O, D'Auria G, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (615 views)
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D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
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Impact Factor: 4.828
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* Exploring the ability of cyclic peptides to target SAM domains: a computational and experimental study (266 views)
Chembiochem (ISSN: 1439-4227linking, 1439-7633), 2020 Mar 2; 21(5): 702-711.
Impact Factor: 2.641
View Export to BibTeX Export to EndNote
Chino M, Maglio O, Nastri F, Pavone V, Degrado WF, Lombardi A
* Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure (640 views)
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2015; 2015(21): 3371-3390.
Impact Factor: 2.686
View Export to BibTeX Export to EndNote
Pannuzzo M, Raudino A, Milardi D, La Rosa C, Karttunen M
* α-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (756 views)
Sci Rep (ISSN: 2045-2322, 2045-2322electronic, 2045-2322linking), 2013; 3: N/D-N/D.
Impact Factor: 5.078
View Export to BibTeX Export to EndNote
Tabbì G, Di Mauro G, Purrello R, Bonomo RP
* Electrochemical characterization of ordered arrays of metallo-porphyrins in aqueous solution (380 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2011 Apr 28; 40(16): 4223-4229.
Impact Factor: 3.838
View Export to BibTeX Export to EndNote
Vagliasindi LI, Arena G, Bonomo RP, Pappalardo G, Tabbì G
* Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein (357 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2011 Mar 21; 40(11): 2441-2450.
Impact Factor: 3.838
View Export to BibTeX Export to EndNote
Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (499 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
View Export to BibTeX Export to EndNote
Banyasz A, Karpati S, Mercier Y, Reguero M, Gustavsson T, Markovitsi D, Improta R
* The peculiar spectral properties of amino-substituted uracils: A combined theoretical and experimental study (350 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Oct 7; 114(39): 12708-12719.
Impact Factor: 3.603
View Export to BibTeX Export to EndNote
Alterio V, Monti SM, Truppo E, Pedone C, Supuran CT, De Simone G
* The first example of a significant active site conformational rearrangement in a carbonic anhydrase-inhibitor adduct: The carbonic anhydrase I-topiramate complex (448 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2010 Sep 7; 8(15): 3528-3533.
Impact Factor: 3.451
View Export to BibTeX Export to EndNote
Mazzaglia A, Micali N, Scolaro LM, Attanasio F, Magrí A, Pappalardo G, Villari V
* Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: A comparative study with two PEG-conjugated variants of the human sequence (441 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Jan 21; 114(2): 705-713.
Impact Factor: 3.603
View Export to BibTeX Export to EndNote
Improta R, Santoro F, Barone V, Lami A
* Vibronic model for the quantum dynamical study of the competition between bright and charge-transfer excited states in single-strand polynucleotides: the adenine dimer case (271 views)
J Phys Chem A (ISSN: 1089-5639, 1520-5215electronic, 1089-5639linking), 2009 Dec 31; 113(52): 15346-15354.
Impact Factor: 2.899
View Export to BibTeX Export to EndNote
Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
* Crystal And Molecular Structure Of Beta-Cyclodextrins Functionalized With The Anti-Inflammatory Drug Etodolac (420 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1227-1235.
Impact Factor: 2.605
View Export to BibTeX Export to EndNote
Improta R, Barone V, Lami A, Santoro F
* Quantum dynamics of the ultrafast ππ*/nπ* population transfer in uracil and 5-fluoro-uracil in water and acetonitrile (289 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2009 Oct 29; 113(43): 14491-14503.
Impact Factor: 3.471
View Export to BibTeX Export to EndNote
Marasco D, Stilo R, Sandomenico A, Monti SM, Tizzano B, De Capua A, Varricchio E, Liguoro D, Zotti T, Formisano S, Ruvo M, Vito P
* Generation And Functional Characterization Of A Bcl10-Inhibitory Peptide That Represses Nf-Kappa B Activation (602 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2009 Sep 15; 422(3): 553-561.
Impact Factor: 5.155
View Export to BibTeX Export to EndNote
Karunakaran V, Kleinermanns K, Improta R, Kovalenko SA
* Photoinduced dynamics of guanosine monophosphate in water from broad-band transient absorption spectroscopy and quantum-chemical calculations (278 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2009; 131(16): 5839-5850.
Impact Factor: 8.58
View Export to BibTeX Export to EndNote
Sgarlata C, Bonaccorso C, Gulino FG, Zito V, Arena G, Sciotto D
* Sterochemistry And Thermodynamics Of The Inclusion Of Aliphatic And Aromatic Anionic Guests In A Tetracationic Calix [4] Arene In Acidic And Neutral Aqueous Solutions (311 views)
New Journal Of Chemistry, 2009; 33: 991-991.
Impact Factor: 3.159
View Export to BibTeX Export to EndNote
Santoro F, Barone V, Improta R
* The Excited States Decay Of The A-T Dna: A Pcm/Td-Dft Study In Aqueous Solution Of The (9-Methyl-Adenine) 2 (1-Methyl-Thymine) 2 Stacked Tetramer (241 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2009; 131(42): 15232-15245.
Impact Factor: 8.58
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Colombo G, Scarabelli G, Romanelli A, Fedone C, Fattorusso R, D'Andrea LD
* Structural determinants of the unusual helix stability of a de novo engineered vascular endothelial growth factor (VEGF) mimicking peptide (470 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2008; 14(14): 4164-4166.
Impact Factor: 5.454
View Export to BibTeX Export to EndNote
Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
* Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues (432 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2005 Dec 23; 12(2): 537-547.
Impact Factor: 4.907
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Zubrzak P, Banas A, Kaczmarek K, Leplawy MT, Sochacki M, Kowalski ML, Szkudlinska B, Zabrocki J, Di Lello P, Isernia C, Saviano M, Pedone C, Benedetti E
* Analogues of cyclolinopeptide A containing alpha-hydroxymethyl amino acid residues (470 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2005; 80(2-3): 347-356.
Impact Factor: 2.425
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Saviano M, Improta R, Benedetti E, Carrozzini B, Cascarano GL, Didierjean C, Toniolo C, Crisma M
* Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue (387 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Apr 2; 5(4): 541-544.
Impact Factor: 3.474
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Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
* Design of a new mimochrome with unique topology (534 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
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Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (384 views)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
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Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
Synthesis, spectroscopic characterisation, and metal ion interaction of a new α-helical peptide (491 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1998; 4(9): 1791-1798.
Impact Factor: 5.153
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Benedetti E, Iacovino R, Pedone C, Rossi F, Saviano M, Isernia C, Montesarchio D, DeNapoli L, Piccialli G
β-Amino acid residues: Conformational characterization of an N- and C-protected homo-β-(S)-leucine (314 views)
Int J Pept Res Ther (ISSN: 0929-5666, 1573-3149), 1997 Jun; 4(3): 129-134.
Impact Factor: 0.557
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Nastri F, Lombardi A, Morelli G, Maglio O, D'Auria G, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (615 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 340-349.
Impact Factor: 4.828
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D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 2. Structural characterization of Co(III) mimochrome I Δ and Λ isomers (489 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 350-362.
Impact Factor: 4.828
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26 Records (24 excluding Abstracts).
Total impact factor: 104.052 (95.815 excluding Abstracts).
Total 5 year impact factor: 111.2 (103.285 excluding Abstracts).
Total impact factor: 104.052 (95.815 excluding Abstracts).
Total 5 year impact factor: 111.2 (103.285 excluding Abstracts).
1135 views. Last view on Saturday 13 May 2023, 1:40:45
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