Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (414 views visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
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Paper type Tipo di articolo: Journal Article,
Impact factor: 1.801, 5-year impact factor Impact factor a 5 anni: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845662273&partnerID=40&md5=c91b9da830e9a36bb0f540ad5eb00a1a
Keywords Parole chiave: Amyloid, Anions, Cations, Counterions, Hofmeister Series, Prion Helix 2 Derived Peptides, Prion Structure, Transmissible Spongiform Encephalopathies, Prion Protein, Prion Protein Helix 2 Derivative, Sodium Chloride, Alpha Helix, Article, Beta Sheet, Human, Ionic Strength, Peptide Synthesis, Priority Journal, Protein Binding, Protein Conformation, Protein Folding, Protein Function, Protein Modification, Amino Acid Sequence, Circular Dichroism, Electrostatics, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Salts, Sulfates,
Affiliations Affiliazioni:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, C.I.R.Pe.B, Università Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
References Riferimenti:
Carrel, R.W., Lomas, D.A., Conformational disease (1997) Lancet, 350, pp. 134-13
Temussi, P.A., Masino, L., Pastore, A., From Alzheimer to Huntington: Why is a structural understanding so difficult? (2003) EMBO J., 22, pp. 355-361
Swietnicki, W., Petersen, R.B., Gambetti, P., Surewicz, W.K., pH-Dependent stability and conformation of the recombinant human prion protein PrP(90-231) (1997) J. Biol. Chem., 272, pp. 27517-27520
Swietnicki, W., Morillas, M., Chen, S.G., Gambetti, P., Surewicz, W.K., Aggregation and fibrillization of the recombinant human prion protein huPrP90-231 (2000) Biochemistry, 39, pp. 424-431
Liemann, S., Glockshuber, R., Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein (1999) Biochemistry, 38, pp. 3258-3267
Hornemann, S., Glockshuber, R., A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH (1998) Proc. Natl. Acad. Sci. U.S.A., 95, pp. 6010-6014
Wildegger, G., Liemann, S., Glockshuber, R., Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates (1999) Nat. Struct. Biol., 6, pp. 550-553
Rezaei, H., Marc, D., Choiset, Y., Takahashi, M., Hoa, G.H.B., Haertle, T., Grosclaude, J., Debey, P., High yield purification and physicochemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility (2000) Eur. J. Biochem., 267, pp. 2833-2839
Zanusso, G., Farinazzo, A., Fiorini, M., Gelati, M., Castagna, A., Righetti, P.G., Rizzuto, N., Monaco, S., pH-Dependent prion protein conformation in classical Creutzfeldt-Jakob disease (2001) J. Biol. Chem., 276, pp. 40377-40380
Baskakov, I.V., Legname, G., Prusiner, S.B., Cohen, F.E., Folding of prion protein to its native α-helical conformation is under kinetic control (2001) J. Biol. Chem., 276, pp. 19687-19690
Morrissey, M.P., Shakhnovich, E.I., Evidence for the role of PrPc helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc. Natl. Acad. Sci. U.S.A., 96, pp. 11293-11298
Apetri, A.C., Surewicz, W.K., Atypical effect of salts on the thermodynamic stability of human prion protein (2003) J. Biol. Chem., 278, pp. 22187-22192
Morillas, M., Vanik, D.L., Surewicz, W.K., On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein (2001) Biochemistry, 40, pp. 6982-6987
Nandi, P.K., Leclerc, E., Marc, D., Unusual property of prion protein unfolding in neutral salt solution (2002) Biochemistry, 41, pp. 11017-11024
Ziegler, J., Sticht, H., Marx, U.C., Müller, W., Rösch, P., Schwarzinger, S., CD and NMR studies of prion protein (PrP) helix 1: Novel implications for its role in the PrPc to PrPSc conversion process (2003) J. Biol. Chem., 278, pp. 50175-50181
Tizzano, B., Palladino, P., De Capua, A., Marasco, D., Rossi, F., Benedetti, E., Pedone, C., Ruvo, M., The human prion protein alpha2 helix: A thermodynamic study of its conformational preferences (2005) Proteins, 59, pp. 72-79
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
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
Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., Strome, R., Fraser, P.E., Kretzschmar, H., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Millhauser, G.L., Copper binding in the prion protein (2004) Acc. Chem. Res., 37, pp. 79-85
Cereghetti, G.M., Schweiger, A., Glockshuber, R., van Doorslaer, S., Stability and Cu(II) binding of prion protein variants related to inherited human prion diseases (2003) Biophys. J., 84, pp. 1985-1997
Zuegg, J., Gready, J.E., Molecular dynamics simulations of human prion protein: Importance of correct treatment of electrostatic interactions (1999) Biochemistry, 38, pp. 13862-13876
Wong, C., Xiong, L.-W., Horiuchi, M., Raymond, L., Wehrly, K., Chesebro, B., Caughey, B., Sulfated glycans and elevated temperature stimulate PrPSc-dependent cell-free formation of protease-resistant prion protein (2001) EMBO J., 20, pp. 377-386
Cordeiro, Y., Machado, F., Juliano Neto, L., Juliano, M.A., Brentani, R.R., Foguel, D., Silva, J.L., DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation (2001) J. Biol. Chem., 276, pp. 49400-49409
Calzolai, L., Zahn, R., Influence of pH on NMR structure and stability of the human prion protein globular domain (2003) J. Biol. Chem., 278, pp. 35592-35596
De Simone, A., Dodson, G.G., Verma, C.S., Zagari, A., Fraternali, F., Prion and water: Tight and dynamical hydration sites have a key role in structural stability (2005) Proc. Natl. Acad. Sci. U.S.A., 102, pp. 7535-7540
Kawatake, S., Nishimura, Y., Sakaguchi, S., Iwaki, T., Doh-ura, K., Surface plasmon resonance analysis for the screening of anti-prion compounds (2006) Biol. Pharm. Bull., 29, pp. 927-932
Collins, K.D., Charge density-dependent strength of hydration and biological structure (1997) Biophys. J., 72, pp. 65-76
Collins, K.D., Ions from the hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process (2004) Methods, 34, pp. 300-311
Niedz, R.P., Evens, T.J., A solution to the problem of ion confounding in experimental biology (2006) Nat. Methods, 3, p. 417
Chen, Y.R., Huang, H.B., Chyan, C.L., Shiao, M.S., Lin, T.H., Chen, Y.C., The effect of Aβ conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy (2006) J. Biochem. (Tokyo), 139, pp. 733-740
Roberts, M.F., Organic compatible solutes of halotolerant and halophilic microorganisms (2005) Saline Syst., 1, pp. 1-30
Arora, A., Ha, C., Park, C.B., Inhibition of insulin amyloid formation by small stress molecules (2004) FEBS Lett., 564, pp. 121-125
Carrel, R. W., Lomas, D. A., Conformational disease (1997) Lancet, 350, pp. 134-13
Temussi, P. A., Masino, L., Pastore, A., From Alzheimer to Huntington: Why is a structural understanding so difficult? (2003) EMBO J., 22, pp. 355-361
Baskakov, I. V., Legname, G., Prusiner, S. B., Cohen, F. E., Folding of prion protein to its native -helical conformation is under kinetic control (2001) J. Biol. Chem., 276, pp. 19687-19690
Morrissey, M. P., Shakhnovich, E. I., Evidence for the role of PrPc helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc. Natl. Acad. Sci. U. S. A., 96, pp. 11293-11298
Apetri, A. C., Surewicz, W. K., Atypical effect of salts on the thermodynamic stability of human prion protein (2003) J. Biol. Chem., 278, pp. 22187-22192
Nandi, P. K., Leclerc, E., Marc, D., Unusual property of prion protein unfolding in neutral salt solution (2002) Biochemistry, 41, pp. 11017-11024
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
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
Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Strome, R., Fraser, P. E., Kretzschmar, H., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Millhauser, G. L., Copper binding in the prion protein (2004) Acc. Chem. Res., 37, pp. 79-85
Cereghetti, G. M., Schweiger, A., Glockshuber, R., van Doorslaer, S., Stability and Cu (II) binding of prion protein variants related to inherited human prion diseases (2003) Biophys. J., 84, pp. 1985-1997
Wong, C., Xiong, L. -W., Horiuchi, M., Raymond, L., Wehrly, K., Chesebro, B., Caughey, B., Sulfated glycans and elevated temperature stimulate PrPSc-dependent cell-free formation of protease-resistant prion protein (2001) EMBO J., 20, pp. 377-386
Collins, K. D., Charge density-dependent strength of hydration and biological structure (1997) Biophys. J., 72, pp. 65-76
Collins, K. D., Ions from the hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process (2004) Methods, 34, pp. 300-311
Niedz, R. P., Evens, T. J., A solution to the problem of ion confounding in experimental biology (2006) Nat. Methods, 3, p. 417
Chen, Y. R., Huang, H. B., Chyan, C. L., Shiao, M. S., Lin, T. H., Chen, Y. C., The effect of A conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy (2006) J. Biochem. (Tokyo), 139, pp. 733-740
Roberts, M. F., Organic compatible solutes of halotolerant and halophilic microorganisms (2005) Saline Syst., 1, pp. 1-30
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 1.801, 5-year impact factor Impact factor a 5 anni: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845662273&partnerID=40&md5=c91b9da830e9a36bb0f540ad5eb00a1a
Keywords Parole chiave: Amyloid, Anions, Cations, Counterions, Hofmeister Series, Prion Helix 2 Derived Peptides, Prion Structure, Transmissible Spongiform Encephalopathies, Prion Protein, Prion Protein Helix 2 Derivative, Sodium Chloride, Alpha Helix, Article, Beta Sheet, Human, Ionic Strength, Peptide Synthesis, Priority Journal, Protein Binding, Protein Conformation, Protein Folding, Protein Function, Protein Modification, Amino Acid Sequence, Circular Dichroism, Electrostatics, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Salts, Sulfates,
Affiliations Affiliazioni:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, C.I.R.Pe.B, Università Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
References Riferimenti:
Carrel, R.W., Lomas, D.A., Conformational disease (1997) Lancet, 350, pp. 134-13
Temussi, P.A., Masino, L., Pastore, A., From Alzheimer to Huntington: Why is a structural understanding so difficult? (2003) EMBO J., 22, pp. 355-361
Swietnicki, W., Petersen, R.B., Gambetti, P., Surewicz, W.K., pH-Dependent stability and conformation of the recombinant human prion protein PrP(90-231) (1997) J. Biol. Chem., 272, pp. 27517-27520
Swietnicki, W., Morillas, M., Chen, S.G., Gambetti, P., Surewicz, W.K., Aggregation and fibrillization of the recombinant human prion protein huPrP90-231 (2000) Biochemistry, 39, pp. 424-431
Liemann, S., Glockshuber, R., Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein (1999) Biochemistry, 38, pp. 3258-3267
Hornemann, S., Glockshuber, R., A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH (1998) Proc. Natl. Acad. Sci. U.S.A., 95, pp. 6010-6014
Wildegger, G., Liemann, S., Glockshuber, R., Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates (1999) Nat. Struct. Biol., 6, pp. 550-553
Rezaei, H., Marc, D., Choiset, Y., Takahashi, M., Hoa, G.H.B., Haertle, T., Grosclaude, J., Debey, P., High yield purification and physicochemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility (2000) Eur. J. Biochem., 267, pp. 2833-2839
Zanusso, G., Farinazzo, A., Fiorini, M., Gelati, M., Castagna, A., Righetti, P.G., Rizzuto, N., Monaco, S., pH-Dependent prion protein conformation in classical Creutzfeldt-Jakob disease (2001) J. Biol. Chem., 276, pp. 40377-40380
Baskakov, I.V., Legname, G., Prusiner, S.B., Cohen, F.E., Folding of prion protein to its native α-helical conformation is under kinetic control (2001) J. Biol. Chem., 276, pp. 19687-19690
Morrissey, M.P., Shakhnovich, E.I., Evidence for the role of PrPc helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc. Natl. Acad. Sci. U.S.A., 96, pp. 11293-11298
Apetri, A.C., Surewicz, W.K., Atypical effect of salts on the thermodynamic stability of human prion protein (2003) J. Biol. Chem., 278, pp. 22187-22192
Morillas, M., Vanik, D.L., Surewicz, W.K., On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein (2001) Biochemistry, 40, pp. 6982-6987
Nandi, P.K., Leclerc, E., Marc, D., Unusual property of prion protein unfolding in neutral salt solution (2002) Biochemistry, 41, pp. 11017-11024
Ziegler, J., Sticht, H., Marx, U.C., Müller, W., Rösch, P., Schwarzinger, S., CD and NMR studies of prion protein (PrP) helix 1: Novel implications for its role in the PrPc to PrPSc conversion process (2003) J. Biol. Chem., 278, pp. 50175-50181
Tizzano, B., Palladino, P., De Capua, A., Marasco, D., Rossi, F., Benedetti, E., Pedone, C., Ruvo, M., The human prion protein alpha2 helix: A thermodynamic study of its conformational preferences (2005) Proteins, 59, pp. 72-79
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
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
Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., Strome, R., Fraser, P.E., Kretzschmar, H., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Millhauser, G.L., Copper binding in the prion protein (2004) Acc. Chem. Res., 37, pp. 79-85
Cereghetti, G.M., Schweiger, A., Glockshuber, R., van Doorslaer, S., Stability and Cu(II) binding of prion protein variants related to inherited human prion diseases (2003) Biophys. J., 84, pp. 1985-1997
Zuegg, J., Gready, J.E., Molecular dynamics simulations of human prion protein: Importance of correct treatment of electrostatic interactions (1999) Biochemistry, 38, pp. 13862-13876
Wong, C., Xiong, L.-W., Horiuchi, M., Raymond, L., Wehrly, K., Chesebro, B., Caughey, B., Sulfated glycans and elevated temperature stimulate PrPSc-dependent cell-free formation of protease-resistant prion protein (2001) EMBO J., 20, pp. 377-386
Cordeiro, Y., Machado, F., Juliano Neto, L., Juliano, M.A., Brentani, R.R., Foguel, D., Silva, J.L., DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation (2001) J. Biol. Chem., 276, pp. 49400-49409
Calzolai, L., Zahn, R., Influence of pH on NMR structure and stability of the human prion protein globular domain (2003) J. Biol. Chem., 278, pp. 35592-35596
De Simone, A., Dodson, G.G., Verma, C.S., Zagari, A., Fraternali, F., Prion and water: Tight and dynamical hydration sites have a key role in structural stability (2005) Proc. Natl. Acad. Sci. U.S.A., 102, pp. 7535-7540
Kawatake, S., Nishimura, Y., Sakaguchi, S., Iwaki, T., Doh-ura, K., Surface plasmon resonance analysis for the screening of anti-prion compounds (2006) Biol. Pharm. Bull., 29, pp. 927-932
Collins, K.D., Charge density-dependent strength of hydration and biological structure (1997) Biophys. J., 72, pp. 65-76
Collins, K.D., Ions from the hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process (2004) Methods, 34, pp. 300-311
Niedz, R.P., Evens, T.J., A solution to the problem of ion confounding in experimental biology (2006) Nat. Methods, 3, p. 417
Chen, Y.R., Huang, H.B., Chyan, C.L., Shiao, M.S., Lin, T.H., Chen, Y.C., The effect of Aβ conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy (2006) J. Biochem. (Tokyo), 139, pp. 733-740
Roberts, M.F., Organic compatible solutes of halotolerant and halophilic microorganisms (2005) Saline Syst., 1, pp. 1-30
Arora, A., Ha, C., Park, C.B., Inhibition of insulin amyloid formation by small stress molecules (2004) FEBS Lett., 564, pp. 121-125
Carrel, R. W., Lomas, D. A., Conformational disease (1997) Lancet, 350, pp. 134-13
Temussi, P. A., Masino, L., Pastore, A., From Alzheimer to Huntington: Why is a structural understanding so difficult? (2003) EMBO J., 22, pp. 355-361
Baskakov, I. V., Legname, G., Prusiner, S. B., Cohen, F. E., Folding of prion protein to its native -helical conformation is under kinetic control (2001) J. Biol. Chem., 276, pp. 19687-19690
Morrissey, M. P., Shakhnovich, E. I., Evidence for the role of PrPc helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc. Natl. Acad. Sci. U. S. A., 96, pp. 11293-11298
Apetri, A. C., Surewicz, W. K., Atypical effect of salts on the thermodynamic stability of human prion protein (2003) J. Biol. Chem., 278, pp. 22187-22192
Nandi, P. K., Leclerc, E., Marc, D., Unusual property of prion protein unfolding in neutral salt solution (2002) Biochemistry, 41, pp. 11017-11024
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
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
Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Strome, R., Fraser, P. E., Kretzschmar, H., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Millhauser, G. L., Copper binding in the prion protein (2004) Acc. Chem. Res., 37, pp. 79-85
Cereghetti, G. M., Schweiger, A., Glockshuber, R., van Doorslaer, S., Stability and Cu (II) binding of prion protein variants related to inherited human prion diseases (2003) Biophys. J., 84, pp. 1985-1997
Wong, C., Xiong, L. -W., Horiuchi, M., Raymond, L., Wehrly, K., Chesebro, B., Caughey, B., Sulfated glycans and elevated temperature stimulate PrPSc-dependent cell-free formation of protease-resistant prion protein (2001) EMBO J., 20, pp. 377-386
Collins, K. D., Charge density-dependent strength of hydration and biological structure (1997) Biophys. J., 72, pp. 65-76
Collins, K. D., Ions from the hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process (2004) Methods, 34, pp. 300-311
Niedz, R. P., Evens, T. J., A solution to the problem of ion confounding in experimental biology (2006) Nat. Methods, 3, p. 417
Chen, Y. R., Huang, H. B., Chyan, C. L., Shiao, M. S., Lin, T. H., Chen, Y. C., The effect of A conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy (2006) J. Biochem. (Tokyo), 139, pp. 733-740
Roberts, M. F., Organic compatible solutes of halotolerant and halophilic microorganisms (2005) Saline Syst., 1, pp. 1-30
Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective
Both theoretical studies and direct experimental evidence have emphasized the importance of electrostatic interactions in the general phenomenon of spontaneous amyloid fibril formation. A number of observations have recently spurred interest in the contribution of these interactions to the conformational behavior of the prion protein. In this paper, we show how salt addition and pH change can modify the conformation of two peptide analogues derived from the human prion protein helix 2 according to a Hofmeister-series-type dependence. Employment of various sodium salts allowed us to highlight the fact that chaotropic anions favor unstructured conformation, whereas kosmotropic anions promote the formation of compact structures like α-helix and β-sheet, which may ultimately facilitate fibril formation. This finding should warn people engaged in ion-based research on prion and derived peptides about cation-bound effects, which have been almost exclusively investigated to date, being easily confounded with modifications that are actually caused by anion activity, thus leading researchers into misunderstand ion-specific effects. To avoid the common complication of ion confounding, it is highly desirable that experiments be designed so that the species causing the modification can be unequivocally perceived. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.
Both theoretical studies and direct experimental evidence have emphasized the importance of electrostatic interactions in the general phenomenon of spontaneous amyloid fibril formation. A number of observations have recently spurred interest in the contribution of these interactions to the conformational behavior of the prion protein. In this paper, we show how salt addition and pH change can modify the conformation of two peptide analogues derived from the human prion protein helix 2 according to a Hofmeister-series-type dependence. Employment of various sodium salts allowed us to highlight the fact that chaotropic anions favor unstructured conformation, whereas kosmotropic anions promote the formation of compact structures like α-helix and β-sheet, which may ultimately facilitate fibril formation. This finding should warn people engaged in ion-based research on prion and derived peptides about cation-bound effects, which have been almost exclusively investigated to date, being easily confounded with modifications that are actually caused by anion activity, thus leading researchers into misunderstand ion-specific effects. To avoid the common complication of ion confounding, it is highly desirable that experiments be designed so that the species causing the modification can be unequivocally perceived. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.
Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective
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Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective
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Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
Dettagli Esporta in BibTeX Esporta in EndNote
Ronga L, Palladino P, Ragone R, Benedetti E, Rossi F
* A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix (267 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009; 15(1): 30-35.
Impact Factor: 1.807
Dettagli Esporta in BibTeX Esporta in EndNote
Ronga L, Palladino P, Costantini S, Facchiano A, Ruvo M, Benedetti E, Ragone R, Rossi F
* Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (527 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
Dettagli Esporta in BibTeX Esporta in EndNote
Ronga L, Tizzano B, Palladino P, Ragone R, Urso E, Maffia M, Ruvo M, Benedetti E, Rossi F
* The prion protein: structural features and related toxic peptides (440 visite)
Chem Biol Drug Des Chemical Biology And Drug Design (ISSN: 1747-0277, 1747-0285), 2006 Sep; 68(3): 139-147.
Impact Factor: 2.507
Dettagli Esporta in BibTeX Esporta in EndNote
4 Records (4 escludendo Abstract e Conferenze).
Impact factor totale: 8.442 (8.442 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 8.969 (8.969 escludendo Abstract e Conferenze).
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