Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (401 views)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
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Paper type: Journal Article,
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Keywords: Amyloidosis, Cellular Prion Protein, Conformational Disorders, Misfolding, Scrapie Prion Isoform, Transmissible Spongiform Encephalopathies, Cell Protein, Metal Ion, Peptide Derivative, Peptide Fragment, Alpha Helix, Amino Acid Sequence, Amino Acid Substitution, Amino Terminal Sequence, Beta Sheet, Brain Spongiosis, Carboxy Terminal Sequence, Human, Huntington Chorea, Metal Binding, Nerve Cell Degeneration, Neurotoxicity, Non Insulin Dependent Diabetes Mellitus, Nonhuman, Parkinson Disease, Point Mutation, Protein Conformation, Protein Domain, Protein Folding, Protein Function, Protein Interaction, Protein Structure, Review, Structure Analysis, Thermodynamics, Titrimetry,
Affiliations:
*** IBB - CNR ***
Dipartimento Delle Scienze Biologiche, C.I.R.Pe.B., Università Federico II, Naples 80134, Italy
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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
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Cobb, N. J., S nnichsen, F. D., McHaourab, H., Surewicz, W. K., Molecular architecture of human prion protein amyloid: A parallel., in-register beta-structure (2007) Proc Natl Acad Sci USA, 104, pp. 18946-18951
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Frankenfield, K. N., Powers, E. T., Kelly, J. W., Influence of the N-terminal domain on the aggregation properties of the prion protein (2005) Protein Sci, 14, pp. 2154-2166
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
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Jobling, M. F., Huang, X., Stewart, L. R., Barnham, K. J., Curtain, C., Volitakis, I., Perugini, M., Cappai, R., Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126 (2001) Biochemistry, 40, pp. 8073-8084
Knaus, K. J., Morillas, M., Swietnicki, W., Malone, M., Surewicz, W. K., Yee, V. C., Crystal structure of the human prion protein reveals a mechanism for oligomerization (2001) Nat Struct Biol, 8, pp. 770-774
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Kuznetsov, I. B., Rackovsky, S., Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations (2004) Protein Sci, 13, pp. 3230-3244
Lee, J. C., Gray, H. B., Winkler, J. R., Copper (II) binding to -synuclein, the Parkinson's protein (2008) J Am Chem Soc, 130, pp. 6898-6899
Lippard, S. J., Berg, J. M., (1994) Principles of Bioinorganic Chemistry, pp. 237-242. , University Science Books, Mill Valley 297-302
Millhauser, G. L., Copper and the prion protein: Methods, structures, function, and disease (2007) Annu Rev Phys Chem, 58, pp. 299-320
Minor Jr, D. L., Kim, P. S., Measurement of the beta-sheet forming propensities of amino acids (1994) Nature, 367, pp. 660-663
Nandi, P. K., Nicole, J. C., Nucleic acid and prion protein interaction produces spherical amyloids which can function in vivo as coats of spongiform encephalopathy agent (2004) J Mol Biol, 344, pp. 827-837
Niedz, R. P., Evens, T. J., A solution to the problem of ion confounding in experimental biology (2006) Nat Methods, 3, p. 417
Pan, K. -H., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Prusiner, S. B., Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins (1993) Proc Natl Acad Sci USA, 90, pp. 10962-10966
Prusiner, S. B., Prions (1998) Proc Natl Acad Sci USA, 95, pp. 13363-13383
Roberts, M. F., Organic compatible solutes of halotolerant and halophilic microorganisms (2005) Saline Syst, 1, pp. 1-30
Shaked, G. M., Shaked, Y., Kariv-Inbal, Z., Halimi, M., Avraham, I., Gabizon, R. A., Protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases (2001) J Biol Chem, 276, pp. 31479-31482
Sundberg, R. J., Martin, R. B., Interactions of histidine and other imidazole derivatives with transition metal ions in chemical and biological systems (1974) Chem Rev, 74, pp. 471-517
Tan, S. Y., Pepys, M. B., (1994) Amyloidosis Histopathology, 25, pp. 403-414
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
Winklhofer, K. F., Heske, J., Heller, U., Reintjes, A., Muranyi, I. M., Tatzelt, J., Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation (2003) J Biol Chem, 278, pp. 14961-14970
Zou, W. -Q., Cashman, N. R., Acidic pH and detergents enhance in vitro conversion of human brain PrPC to a PrPSc-like form (2002) J Biol Chem, 277, pp. 43942-43947
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
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Keywords: Amyloidosis, Cellular Prion Protein, Conformational Disorders, Misfolding, Scrapie Prion Isoform, Transmissible Spongiform Encephalopathies, Cell Protein, Metal Ion, Peptide Derivative, Peptide Fragment, Alpha Helix, Amino Acid Sequence, Amino Acid Substitution, Amino Terminal Sequence, Beta Sheet, Brain Spongiosis, Carboxy Terminal Sequence, Human, Huntington Chorea, Metal Binding, Nerve Cell Degeneration, Neurotoxicity, Non Insulin Dependent Diabetes Mellitus, Nonhuman, Parkinson Disease, Point Mutation, Protein Conformation, Protein Domain, Protein Folding, Protein Function, Protein Interaction, Protein Structure, Review, Structure Analysis, Thermodynamics, Titrimetry,
Affiliations:
*** IBB - CNR ***
Dipartimento Delle Scienze Biologiche, C.I.R.Pe.B., Università Federico II, Naples 80134, Italy
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Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain
The mechanism that underlies a multitude of human disorders, including type II diabetes, Parkinson's, Huntington's and Alzheimer's, and the prion encephalopathies, is beta-structure expansion through a pathogenic aggregation-prone monomeric form. beta-sheet expansion disorders share intermolecular association as a common determinant, being therefore collectively identified as conformational diseases, but little is known about the underlying mechanism. Transmissible spongiform encephalopathies, also known as prion diseases, are all characterised by progressive neuronal degeneration associated to marked extracellular accumulation of an amyloidogenic conformer of the normal cellular prion protein (PrP(C)), referred to as the scrapie isoform (PrP(Sc)), which is thought to be responsible for the disease symptoms. PrP(C) is a ubiquitous 231-amino acid glycoprotein, whose physiological role is still elusive. It is organised as an N-terminal disordered region and a compact C-terminal domain, where secondary structure elements consist of three alpha-helices (alpha 1, alpha 2 and alpha 3), with an alpha 2-alpha 3 disulphide bridge, and two short beta-strands (beta 1 and beta 2). Evidence accumulated so far suggests that the protein possesses one or several 'spots' of intrinsic conformational weakness, which may trigger generic folding, leading the whole architecture to adopt aggregation-prone conformations. One of such spots is suspected to be the C-terminal side of the alpha-helix 2, which has recently gained the attention of several investigations because it gathers several disease-associated point mutations, can be strongly fibrillogenic and toxic to neuronal cells, and possesses chameleon conformational behaviour. This paper briefly reviews recent literature on alpha-2 domain-derived model peptides.
The mechanism that underlies a multitude of human disorders, including type II diabetes, Parkinson's, Huntington's and Alzheimer's, and the prion encephalopathies, is beta-structure expansion through a pathogenic aggregation-prone monomeric form. beta-sheet expansion disorders share intermolecular association as a common determinant, being therefore collectively identified as conformational diseases, but little is known about the underlying mechanism. Transmissible spongiform encephalopathies, also known as prion diseases, are all characterised by progressive neuronal degeneration associated to marked extracellular accumulation of an amyloidogenic conformer of the normal cellular prion protein (PrP(C)), referred to as the scrapie isoform (PrP(Sc)), which is thought to be responsible for the disease symptoms. PrP(C) is a ubiquitous 231-amino acid glycoprotein, whose physiological role is still elusive. It is organised as an N-terminal disordered region and a compact C-terminal domain, where secondary structure elements consist of three alpha-helices (alpha 1, alpha 2 and alpha 3), with an alpha 2-alpha 3 disulphide bridge, and two short beta-strands (beta 1 and beta 2). Evidence accumulated so far suggests that the protein possesses one or several 'spots' of intrinsic conformational weakness, which may trigger generic folding, leading the whole architecture to adopt aggregation-prone conformations. One of such spots is suspected to be the C-terminal side of the alpha-helix 2, which has recently gained the attention of several investigations because it gathers several disease-associated point mutations, can be strongly fibrillogenic and toxic to neuronal cells, and possesses chameleon conformational behaviour. This paper briefly reviews recent literature on alpha-2 domain-derived model peptides.
Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain
| ▼ Biochemical and functional characterization of intrinsically disordered proteins (IDPs) in human diseases |
Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain
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View Export to BibTeX Export to EndNote
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Abdom Imaging (ISSN: 0942-8925, 1432-0509), 2003 Sep; 28(5): 688-690.
Impact Factor: 0.996
View Export to BibTeX Export to EndNote
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Impact Factor: 3.992
View Export to BibTeX Export to EndNote
Mainenti PP, Petrelli G, Lamanda R, Amalfi G, Castiglione F
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J Clin Gastroenterol (ISSN: 0192-0790), 1997 Apr; 24(3): 173-175.
Impact Factor: 0.936
View Export to BibTeX Export to EndNote
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Total 5 year impact factor: 66.278 (61.865 excluding Abstracts).
Total impact factor: 64.434 (59.915 excluding Abstracts).
Total 5 year impact factor: 66.278 (61.865 excluding Abstracts).
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