NMR structure and CD titration with metal cations of human prion α2-helix-related peptides(468 views) Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R, Rossi F
Dipartimento delle Scienze Biologiche, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Scienze e Tecnologie per l'Ambiente e il Territorio, Università del Molise, Contrada Fonte Lappone, 86090 Pesche, Italy
Istituto di Chimica Biomolecolare, CNR, Via Campi Flegrei 34, 80078 Pozzuoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Santa Maria di Costantinopoli 16, 80138 Napoli, Italy
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Jackson, G. S., Clarke, A. R., Mammalian prion proteins (2000) Current Opinion in Structural Biology, 10 (1), pp. 69-74. , a. r. clarke@sm. ic. ac. u
Cohen, F. E., Prusiner, S. B., Pathologic conformations of prion proteins (1998) Annual Review of Biochemistry, 67, pp. 793-819. , cohen@cgl. ucsf. edu
Kocisko, D. A., Come, J. H., Priola, S. A., Cell-free formation of protease-resistant prion protein (1994) Nature, 370 (6489), pp. 471-474
Kocisko, D. A., Priola, S. A., Raymond, G. J., Chesebro, B., Lansbury Jr., P. T., Caughey, B., Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier (1995) Proceedings of the National Academy of Sciences of the United States of America, 92 (9), pp. 3923-3927
Prusiner, S. B., Prions (1998) Proceedings of the National Academy of Sciences of the United States of America, 95 (23), pp. 13363-13383
Scott, M. R., Will, R., Ironside, J., Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans (1999) Proceedings of the National Academy of Sciences of the United States of America, 96 (26), pp. 15137-15142
Kelly, J. W., The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways (1998) Current Opinion in Structural Biology, 8 (1), pp. 101-106. , jkelly@scripps. edu
Fern ndez, A., Scheraga, H. A., Insufficiently dehydrated hydrogen bonds as determinants of protein interactions (2003) Proceedings of the National Academy of Sciences of the United States of America, 100 (1), pp. 113-118. , has5@cornell. edu
Bosques, C. J., Imperiali, B., The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment (2003) Proceedings of the National Academy of Sciences of the United States of America, 100 (13), pp. 7593-7598. , imper@mit. edu
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) Journal of Inorganic Biochemistry, 98 (1), pp. 133-143. , erizzarelli@dipchi. unict. it
Jackson, G. S., Hosszu, L. L. P., Power, A., Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations (1999) Science, 283 (5409), pp. 1935-1937
DuBay, K. F., Pawar, A. P., Chiti, F., Zurdo, J., Dobson, C. M., Vendruscolo, M., Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains (2004) Journal of Molecular Biology, 341 (5), pp. 1317-1326. , cmd44@cam. ac. uk mv245@cam. ac. uk
Dima, R. I., Thirumalai, D., Exploring the propensities of helices in (2002) Biophysical Journal, 83 (3), pp. 1268-1280. , PrPC to form sheet using NMR structures and sequence alignments
Prusiner, S. B., Molecular biology and pathogenesis of prion diseases (1996) Trends in Biochemical Sciences, 21 (12), pp. 482-487
Shamsir, M. S., Dalby, A. R., One gene, two diseases and three conformations: molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures (2005) Proteins: Structure, Function, and Bioinformatics, 59 (2), pp. 275-290. , a. r. dalby@exeter. ac. uk
Bax, A., Davis, D. G., MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy (1985) Journal of Magnetic Resonance, 65 (2), pp. 355-360
Rance, M., S rensen, O. W., Bodenhausen, G., Wagner, G., Ernst, R. R., W thrich, K., Improved spectral resolution in cosy (1983) Biochemical and Biophysical Research Communications, 117 (2), pp. 479-485. , H1 NMR spectra of proteins via double quantum filtering
Johnson, B. A., Blevins, R. A., NMR view: a computer program for the visualization and analysis of NMR data (1994) Journal of Biomolecular NMR, 4 (5), pp. 603-614
W thrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley New York, NY, USA
G ntert, P., Braun, W., W thrich, K., Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA (1991) Journal of Molecular Biology, 217 (3), pp. 517-530
G ntert, P., Mumenthaler, C., W thrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) Journal of Molecular Biology, 273 (1), pp. 283-298
Jackson, G. S., Collinge, J., The molecular pathology of CJD: old and new variants (2001) Journal of Clinical Pathology, 54 (6), pp. 393-399
Millhauser, G. L., Copper binding in the prion protein (2004) Accounts of Chemical Research, 37 (2), pp. 79-85. , glennm@hydrogen. ucsc. edu
NMR structure and CD titration with metal cations of human prion α2-helix-related peptides
The 173-195 segment corresponding to the helix 2 of the C-globular prion protein domain could be one of several "spots" of intrinsic conformational flexibility. In fact, it possesses chameleon conformational behaviour and gathers several disease-associated point mutations. We have performed spectroscopic studies on the wild-type fragment 173-195 and on its D178N mutant dissolved in trifluoroethanol to mimic the in vivo system, both in the presence and in the absence of metal cations. NMR data showed that the structure of the D178N mutant is characterized by two short helices separated by a kink, whereas the wild-type peptide is fully helical. Both peptides retained these structural organizations, as monitored by CD, in the presence of metal cations. NMR spectra were however not in favour of the formation of definite ion-peptide complexes. This agrees with previous evidence that other regions of the prion protein are likely the natural target of metal cation binding.
NMR structure and CD titration with metal cations of human prion α2-helix-related peptides
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