DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes (377 views)
New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.44, 5-year impact factor: 2.837
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0035672068&partnerID=40&md5=ad6fb54f41695d3ce1b0885c116e95b9
Keywords: 2 Dipalmitoyl Sn Glycero 3 Phosphocholine, 2 Dipalmitoyl Sn Glycero 3 Phosphoethanolamine, Choline Derivative, Ethanolamine Derivative, Hydrocarbon, Lipid, Peptide, Prion Protein, Unclassified Drug, Article, Artificial Membrane, Binding Affinity, Cell Surface, Differential Scanning Calorimetry, Enthalpy, Hydrophobicity, Lipid Bilayer, Membrane Binding, Membrane Model, Prion Disease, Priority Journal, Protein Interaction, Surface Property, Temperature,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita' di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
References:
Prusiner, S.B., (1991) Science, 252, p. 151
Bolton, D.C., McKinley, M.P., Prusiner, S.B., (1982) Science, 218, p. 1309
McKinley, M.P., Bolton, D.C., Prusiner, S.B., (1983) Cell, 35, p. 57
De Armond, S.J., McKinley, M.P., Barry, R.A., Braunfeld, M.B., McColloch, J.R., Prusiner, S.B., (1985) Cell, 41, p. 221
Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., Tagliavini, F., (1993) Nature, 362, p. 543
Forloni, G., Del Bo, R., Angeretti, N., Chiesa, R., Smiroldo, S., Doni, R., Ghibaudi, E., Verga, L., (1994) Eur. J. Neurosci., 6, p. 1415
Brown, D.R., Schmidt, B., Kretzschmar, H.A., (1996) Nature, 380, p. 345
Riek, R., Hornemann, S., Wilder, G., Billeter, M., Glockshuber, R., Wuthrich, K., (1996) Nature, 382, p. 180
Donne, D.G., Viles, J.H., Groth, D., Mehlhorn, I., James, T.L., Cohen, F.E., Prusiner, S.B., Dyson, H.J., (1997) Proc. Natl. Acad. Sci. U. S. A., 94, p. 13452
Caughey, B.W., Dong, A., Bhat, K.S., Trust, D., Caughey, W.S., (1991) Biochemistry, 30, p. 7672
Pan, K.M., Baldwin, M.A., Nguyen, J.T., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Prusiner, S.B., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, p. 10962
Safar, J., Roller, P.P., Gajdusek, D.C., Gibbs C.J., Jr., (1993) J. Biol. Chem., 268, p. 20276
Viret, J., Dormont, D., Molle, D., Court, L., Leterrier, F., Cathala, F., Gibbs C.J., Jr., Gajdusek, D.C., (1981) Biochem. Biophys. Res. Commun., 101, p. 830
Kristensson, K., Feurstein, B., Taraboulos, A., Hyun, W.C., Prusiner, S.B., De Armond, S.J., (1993) Neurology, 43, p. 2335
Wong, K., Qiu, Y., Hyun, W., Nixon, R., Vancleef, J., Sanchez-Salazar, J., Prusiner, S.B., De Armond, S.J., (1996) Neurology, 47, p. 741
Giaccone, G., Verga, L., Bugiani, O., Frangione, B., Serban, D., Prusiner, S.B., Forlow, M.R., Tagliavini, F., (1992) Proc. Natl. Acad. Sci. U. S. A., 89, p. 9349
Muramoto, T., Scott, M., Cohen, F.E., Prusiner, S.B., (1996) Proc. Natl. Acad. Sci. U. S. A., 93, p. 15457
Supattapone, S., Bousque, P., Muramoto, T., Wille, H., Aagaard, C., Peretz, D., Nguyen, H.O., Scott, M., (1999) Cell, 96, p. 869
Holscher, C., Delius, H., Burkle, A., (1998) J. Virol., 72, p. 1153
Brown, D.R., Herms, J., Kretzschmar, H.A., (1994) Neurology, 5, p. 2057
Jobling, M.J., Stewart, L.R., White, A.R., McLean, C., Friedhuber, A., Maher, F., Beyreuter, K., Neurochem, J., (1999), 73, p. 1557Kuntz, B., Sandmeyer, E., Christen, P., (1999) FEBS Lett., 485, p. 65
Brown, D.R., (1999) FEBS Lett., 460, p. 559
Forloni, G., Salmona, M., Bugiani, O., Tagliavini, F., (2000) FEBS Lett., 466, p. 205
Chapman, D., (1982) Biological Membranes, 4, p. 179. , Academic Press, New York
Lohner, K., Prenner, E.J., (1999) Biochim. Biophys. Acta, 1462, p. 14
Yorek, M.A., (1993) Phospholipid Handbook, p. 745. , ed. G. Cevc, Marcel Dekker, New York
Mayer, L.D., Hope, M.J., Cullis, P.R., Janoff, A.S., (1985) Biochim. Biophys. Acta, 817, p. 193
MacDonald, R.C., MacDonald, R.I., Menco, M., Takeshita, K., Subarrao, N.K., Hu, L., (1991) Biochim. Biophys. Acta, 1061, p. 297
Antunes-Madeira, M.C., Videira, R.A., Madeira, V.M.C., (1994) Biochim. Biophys. Acta, 1190, p. 149
Heimburg, T., (1998) Biochim. Biophys. Acta, 1415, p. 147
Hinz, H.J., Sturtevant, J.M., (1972) J. Biol. Chem., 247, p. 6071
Mouritsen, O.G., Bloom, M., (1984) Biophys. J., 46, p. 141
Hunter, G.D., (1969) Biochem. J., p. 114. , 22p
Meda, L., Cassatella, M., Szendrei, G.I., Oltvos L., Jr., Baron, P., Villalba, M., Ferrari, D., Rossi, F., (1995) Nature, 374, p. 647
Selvaggini, C., De Gioia, L., Cantù, L., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Salmona, M., (1993) Biochem. Biophys. Res. Commun., 194, p. 1380
De Gioia, L., Selvaggini, C., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Tagliavini, F., Salmona, M., (1994) J. Biol. Chem., 269, p. 1
Bugiani, O., Diomede, L., Algeri, M., De Gioia, L., Florio, T., Schettini, G., Tagliavini, F., Salmona, M., (1995) J. Neuropathol. Exp. Neurol., 54, p. 449
Verkleij, A.J., Zwaal, R.F., Roelofsen, B., Comfurius, P., Kastelijn, D., Deenen, L.V., (1973) Biochim. Biophys. Acta, 323, p. 178
Prusiner, S. B., (1991) Science, 252, p. 151
Bolton, D. C., McKinley, M. P., Prusiner, S. B., (1982) Science, 218, p. 1309
McKinley, M. P., Bolton, D. C., Prusiner, S. B., (1983) Cell, 35, p. 57
De Armond, S. J., McKinley, M. P., Barry, R. A., Braunfeld, M. B., McColloch, J. R., Prusiner, S. B., (1985) Cell, 41, p. 221
Brown, D. R., Schmidt, B., Kretzschmar, H. A., (1996) Nature, 380, p. 345
Donne, D. G., Viles, J. H., Groth, D., Mehlhorn, I., James, T. L., Cohen, F. E., Prusiner, S. B., Dyson, H. J., (1997) Proc. Natl. Acad. Sci. U. S. A., 94, p. 13452
Caughey, B. W., Dong, A., Bhat, K. S., Trust, D., Caughey, W. S., (1991) Biochemistry, 30, p. 7672
Pan, K. M., Baldwin, M. A., Nguyen, J. T., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Prusiner, S. B., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, p. 10962
Brown, D. R., Herms, J., Kretzschmar, H. A., (1994) Neurology, 5, p. 2057
Jobling, M. J., Stewart, L. R., White, A. R., McLean, C., Friedhuber, A., Maher, F., Beyreuter, K., Neurochem, J., (1999), 73, p. 1557Kuntz, B., Sandmeyer, E., Christen, P., (1999) FEBS Lett., 485, p. 65
Brown, D. R., (1999) FEBS Lett., 460, p. 559
Yorek, M. A., (1993) Phospholipid Handbook, p. 745. , ed. G. Cevc, Marcel Dekker, New York
Mayer, L. D., Hope, M. J., Cullis, P. R., Janoff, A. S., (1985) Biochim. Biophys. Acta, 817, p. 193
MacDonald, R. C., MacDonald, R. I., Menco, M., Takeshita, K., Subarrao, N. K., Hu, L., (1991) Biochim. Biophys. Acta, 1061, p. 297
Hinz, H. J., Sturtevant, J. M., (1972) J. Biol. Chem., 247, p. 6071
Mouritsen, O. G., Bloom, M., (1984) Biophys. J., 46, p. 141
Hunter, G. D., (1969) Biochem. J., p. 114. , 22p
Verkleij, A. J., Zwaal, R. F., Roelofsen, B., Comfurius, P., Kastelijn, D., Deenen, L. V., (1973) Biochim. Biophys. Acta, 323, p. 178
New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.44, 5-year impact factor: 2.837
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0035672068&partnerID=40&md5=ad6fb54f41695d3ce1b0885c116e95b9
Keywords: 2 Dipalmitoyl Sn Glycero 3 Phosphocholine, 2 Dipalmitoyl Sn Glycero 3 Phosphoethanolamine, Choline Derivative, Ethanolamine Derivative, Hydrocarbon, Lipid, Peptide, Prion Protein, Unclassified Drug, Article, Artificial Membrane, Binding Affinity, Cell Surface, Differential Scanning Calorimetry, Enthalpy, Hydrophobicity, Lipid Bilayer, Membrane Binding, Membrane Model, Prion Disease, Priority Journal, Protein Interaction, Surface Property, Temperature,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita' di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
References:
Prusiner, S.B., (1991) Science, 252, p. 151
Bolton, D.C., McKinley, M.P., Prusiner, S.B., (1982) Science, 218, p. 1309
McKinley, M.P., Bolton, D.C., Prusiner, S.B., (1983) Cell, 35, p. 57
De Armond, S.J., McKinley, M.P., Barry, R.A., Braunfeld, M.B., McColloch, J.R., Prusiner, S.B., (1985) Cell, 41, p. 221
Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., Tagliavini, F., (1993) Nature, 362, p. 543
Forloni, G., Del Bo, R., Angeretti, N., Chiesa, R., Smiroldo, S., Doni, R., Ghibaudi, E., Verga, L., (1994) Eur. J. Neurosci., 6, p. 1415
Brown, D.R., Schmidt, B., Kretzschmar, H.A., (1996) Nature, 380, p. 345
Riek, R., Hornemann, S., Wilder, G., Billeter, M., Glockshuber, R., Wuthrich, K., (1996) Nature, 382, p. 180
Donne, D.G., Viles, J.H., Groth, D., Mehlhorn, I., James, T.L., Cohen, F.E., Prusiner, S.B., Dyson, H.J., (1997) Proc. Natl. Acad. Sci. U. S. A., 94, p. 13452
Caughey, B.W., Dong, A., Bhat, K.S., Trust, D., Caughey, W.S., (1991) Biochemistry, 30, p. 7672
Pan, K.M., Baldwin, M.A., Nguyen, J.T., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Prusiner, S.B., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, p. 10962
Safar, J., Roller, P.P., Gajdusek, D.C., Gibbs C.J., Jr., (1993) J. Biol. Chem., 268, p. 20276
Viret, J., Dormont, D., Molle, D., Court, L., Leterrier, F., Cathala, F., Gibbs C.J., Jr., Gajdusek, D.C., (1981) Biochem. Biophys. Res. Commun., 101, p. 830
Kristensson, K., Feurstein, B., Taraboulos, A., Hyun, W.C., Prusiner, S.B., De Armond, S.J., (1993) Neurology, 43, p. 2335
Wong, K., Qiu, Y., Hyun, W., Nixon, R., Vancleef, J., Sanchez-Salazar, J., Prusiner, S.B., De Armond, S.J., (1996) Neurology, 47, p. 741
Giaccone, G., Verga, L., Bugiani, O., Frangione, B., Serban, D., Prusiner, S.B., Forlow, M.R., Tagliavini, F., (1992) Proc. Natl. Acad. Sci. U. S. A., 89, p. 9349
Muramoto, T., Scott, M., Cohen, F.E., Prusiner, S.B., (1996) Proc. Natl. Acad. Sci. U. S. A., 93, p. 15457
Supattapone, S., Bousque, P., Muramoto, T., Wille, H., Aagaard, C., Peretz, D., Nguyen, H.O., Scott, M., (1999) Cell, 96, p. 869
Holscher, C., Delius, H., Burkle, A., (1998) J. Virol., 72, p. 1153
Brown, D.R., Herms, J., Kretzschmar, H.A., (1994) Neurology, 5, p. 2057
Jobling, M.J., Stewart, L.R., White, A.R., McLean, C., Friedhuber, A., Maher, F., Beyreuter, K., Neurochem, J., (1999), 73, p. 1557Kuntz, B., Sandmeyer, E., Christen, P., (1999) FEBS Lett., 485, p. 65
Brown, D.R., (1999) FEBS Lett., 460, p. 559
Forloni, G., Salmona, M., Bugiani, O., Tagliavini, F., (2000) FEBS Lett., 466, p. 205
Chapman, D., (1982) Biological Membranes, 4, p. 179. , Academic Press, New York
Lohner, K., Prenner, E.J., (1999) Biochim. Biophys. Acta, 1462, p. 14
Yorek, M.A., (1993) Phospholipid Handbook, p. 745. , ed. G. Cevc, Marcel Dekker, New York
Mayer, L.D., Hope, M.J., Cullis, P.R., Janoff, A.S., (1985) Biochim. Biophys. Acta, 817, p. 193
MacDonald, R.C., MacDonald, R.I., Menco, M., Takeshita, K., Subarrao, N.K., Hu, L., (1991) Biochim. Biophys. Acta, 1061, p. 297
Antunes-Madeira, M.C., Videira, R.A., Madeira, V.M.C., (1994) Biochim. Biophys. Acta, 1190, p. 149
Heimburg, T., (1998) Biochim. Biophys. Acta, 1415, p. 147
Hinz, H.J., Sturtevant, J.M., (1972) J. Biol. Chem., 247, p. 6071
Mouritsen, O.G., Bloom, M., (1984) Biophys. J., 46, p. 141
Hunter, G.D., (1969) Biochem. J., p. 114. , 22p
Meda, L., Cassatella, M., Szendrei, G.I., Oltvos L., Jr., Baron, P., Villalba, M., Ferrari, D., Rossi, F., (1995) Nature, 374, p. 647
Selvaggini, C., De Gioia, L., Cantù, L., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Salmona, M., (1993) Biochem. Biophys. Res. Commun., 194, p. 1380
De Gioia, L., Selvaggini, C., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Tagliavini, F., Salmona, M., (1994) J. Biol. Chem., 269, p. 1
Bugiani, O., Diomede, L., Algeri, M., De Gioia, L., Florio, T., Schettini, G., Tagliavini, F., Salmona, M., (1995) J. Neuropathol. Exp. Neurol., 54, p. 449
Verkleij, A.J., Zwaal, R.F., Roelofsen, B., Comfurius, P., Kastelijn, D., Deenen, L.V., (1973) Biochim. Biophys. Acta, 323, p. 178
Prusiner, S. B., (1991) Science, 252, p. 151
Bolton, D. C., McKinley, M. P., Prusiner, S. B., (1982) Science, 218, p. 1309
McKinley, M. P., Bolton, D. C., Prusiner, S. B., (1983) Cell, 35, p. 57
De Armond, S. J., McKinley, M. P., Barry, R. A., Braunfeld, M. B., McColloch, J. R., Prusiner, S. B., (1985) Cell, 41, p. 221
Brown, D. R., Schmidt, B., Kretzschmar, H. A., (1996) Nature, 380, p. 345
Donne, D. G., Viles, J. H., Groth, D., Mehlhorn, I., James, T. L., Cohen, F. E., Prusiner, S. B., Dyson, H. J., (1997) Proc. Natl. Acad. Sci. U. S. A., 94, p. 13452
Caughey, B. W., Dong, A., Bhat, K. S., Trust, D., Caughey, W. S., (1991) Biochemistry, 30, p. 7672
Pan, K. M., Baldwin, M. A., Nguyen, J. T., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Prusiner, S. B., (1993) Proc. Natl. Acad. Sci. U. S. A., 90, p. 10962
Brown, D. R., Herms, J., Kretzschmar, H. A., (1994) Neurology, 5, p. 2057
Jobling, M. J., Stewart, L. R., White, A. R., McLean, C., Friedhuber, A., Maher, F., Beyreuter, K., Neurochem, J., (1999), 73, p. 1557Kuntz, B., Sandmeyer, E., Christen, P., (1999) FEBS Lett., 485, p. 65
Brown, D. R., (1999) FEBS Lett., 460, p. 559
Yorek, M. A., (1993) Phospholipid Handbook, p. 745. , ed. G. Cevc, Marcel Dekker, New York
Mayer, L. D., Hope, M. J., Cullis, P. R., Janoff, A. S., (1985) Biochim. Biophys. Acta, 817, p. 193
MacDonald, R. C., MacDonald, R. I., Menco, M., Takeshita, K., Subarrao, N. K., Hu, L., (1991) Biochim. Biophys. Acta, 1061, p. 297
Hinz, H. J., Sturtevant, J. M., (1972) J. Biol. Chem., 247, p. 6071
Mouritsen, O. G., Bloom, M., (1984) Biophys. J., 46, p. 141
Hunter, G. D., (1969) Biochem. J., p. 114. , 22p
Verkleij, A. J., Zwaal, R. F., Roelofsen, B., Comfurius, P., Kastelijn, D., Deenen, L. V., (1973) Biochim. Biophys. Acta, 323, p. 178
DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes
The incorporation of the human prion peptide PrP106-126 into 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine (DPPE) host model membranes has been investigated by differential scanning calorimetry. Two different types of peptide-membrane interactions have been studied. In one case, the peptide is obliged to be included into the hydrocarbon region of the lipid bilayer, in the other case, it is allowed to interact with the external surface of the membrane. The PrP106-126 incorporated into the DPPC membrane shows an increase in the gel-liquid crystal transition temperature of the bilayer with a decreased enthalpy change. The "oriented" insertion of the hydrophobic part of the fragment into the bilayer, with a consequent increase in the order of the lipidic hydrocarbon chains in the gel state, is responsible for this behavior. Independently from the procedure adopted for the preparation of the sample, the PrP106-126 fragment interacts strongly and irreversibly with the host membrane. In contrast, when PrP106-126 is incorporated in the DPPE model membrane, the gel-liquid crystal transition temperature of the bilayer and the associated enthalpy change decrease. When added externally to the DPPE model membrane, the PrP106-126 fragment has no effect on the phase behavior of the bilayer. These findings suggest that PrP106-126 has a specific affinity for DPPC membranes that might correspond to the external surface of cells.
The incorporation of the human prion peptide PrP106-126 into 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine (DPPE) host model membranes has been investigated by differential scanning calorimetry. Two different types of peptide-membrane interactions have been studied. In one case, the peptide is obliged to be included into the hydrocarbon region of the lipid bilayer, in the other case, it is allowed to interact with the external surface of the membrane. The PrP106-126 incorporated into the DPPC membrane shows an increase in the gel-liquid crystal transition temperature of the bilayer with a decreased enthalpy change. The "oriented" insertion of the hydrophobic part of the fragment into the bilayer, with a consequent increase in the order of the lipidic hydrocarbon chains in the gel state, is responsible for this behavior. Independently from the procedure adopted for the preparation of the sample, the PrP106-126 fragment interacts strongly and irreversibly with the host membrane. In contrast, when PrP106-126 is incorporated in the DPPE model membrane, the gel-liquid crystal transition temperature of the bilayer and the associated enthalpy change decrease. When added externally to the DPPE model membrane, the PrP106-126 fragment has no effect on the phase behavior of the bilayer. These findings suggest that PrP106-126 has a specific affinity for DPPC membranes that might correspond to the external surface of cells.
DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes
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DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes
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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 (416 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1227-1235.
Impact Factor: 2.605
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De Capua A, Goodman M, Amino Y, Saviano M, Benedetti E
* Conformation analysis of aspartame-based sweeteners by NMR spectroscopy, molecular dynamics simulations, and X-ray diffraction studies (614 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2006 Feb; 7(2): 377-387.
Impact Factor: 4.1
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Arena G, Contino A, Longo E, Sgarlata C, Spoto G, Zito V
* Self-assembling, patterning and SPR imaging of a 1, 3 alternate bis(dipyridyl)calix[4] arene derivative - Cu2+ complex immobilized on to Au(111) surfaces (327 views)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2004; 10(16): 1812-1813.
Impact Factor: 3.997
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Nastri F, Lombardi A, D'Andrea LD, Sanseverino M, Maglio O, Pavone V
Miniaturized hemoproteins (423 views)
Biopolymers (ISSN: 0006-3525print, 0006-3525linking, 1097-0282electronic), 1998; 47(1): 5-22.
Impact Factor: 2.086
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8 Records (8 excluding Abstracts).
Total impact factor: 24.706 (24.706 excluding Abstracts).
Total 5 year impact factor: 26.165 (26.165 excluding Abstracts).
Total impact factor: 24.706 (24.706 excluding Abstracts).
Total 5 year impact factor: 26.165 (26.165 excluding Abstracts).
377 views. Last view on Saturday 14 January 2023, 17:41:53
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