Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides
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Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (160 visite)

Ronga L, Palladino P, Costantini S, Facchiano A, Ruvo M, Benedetti E, Ragone R, Rossi F

Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 83-90.



Tipo di articolo: Journal Article,

Impact factor: 3.259, Impact factor a 5 anni: 3.641

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847296574&partnerID=40&md5=7b79d68467c13d854285e64f32260cbc

Parole chiave: Amyloid, Copper Binding Protein, N-Linked Glycoprotein, Prion Structure, Prion Toxicity, Transmissible Spongiform Encephalopathies, Amyloid Protein, Antibiotic Agent, Metal Ion, Polyamine Derivative, Polyanion, Polyene Antibiotic Agent, Polypeptide, Prion Protein, Proteinase, Tetracycline, Tetrapyrrole Derivative, Alpha Helix, Amino Terminal Sequence, Beta Sheet, Carboxy Terminal Sequence, Cell Function, Central Nervous System Disease, Conformational Transition, Copper Metabolism, Drug Protein Binding, Enzyme Inhibition, Human, Mammal Cell, Metal Binding, Neuropathology, Nonhuman, Oxidative Stress, Prion Disease, Protein Domain, Protein Expression, Protein Secondary Structure, Review, Scrapie, Species Conservation, Structure Activity Relation, Amino Acid Sequence, Animals, Models, Molecular, Molecular Sequence Data, Nerve Degeneration, Protein Conformation, Protein Structure, Tertiary, Thermodynamics,

Affiliazioni:

*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, Università Federico II di Napoli, Istituto di Biostrutture e Bioimmagini, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
Istituto di Scienze dell'Alimentazione, CNR, 83100 Avellino, Italy


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The physiological form of the prion protein is normally expressed in mammalian cell and is highly conserved among species, although its role in cellular function remains elusive. Available evidence suggests that this protein is essential for neuronal integrity in the brain, possibly with a role in copper metabolism and cellular response to oxidative stress. In prion diseases, the benign cellular form of the protein is converted into an insoluble, protease-resistant abnormal scrapie form. This conversion parallels a conformational change of the polypeptide from a predominantly a-helical to a highly P-sheet secondary structure. The scrapie form accumulates in the central nervous system of affected individuals, and its protease-resistant core aggregates into amyloid Fibrils outside the cell. The pathogenesis and molecular basis of the nerve cell loss that accompanies this process are not understood. Limited structural information is available on aggregate formation by this protein as the possible cause of these diseases and on its toxicity. A large amount of structure-activity studies is based on the prion fragment approach, but the resulting information is often difficult to untangle. This overview focuses on the most relevant structural and functional aspects of the prion-induced conformational disease linked to peptides derived from the unstructured N-terminal and globular C-terminal domains.
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1161-1171.
Impact Factor: 2.605
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Capparelli R, Romanelli A, Iannaccone M, Nocerino N, Ripa R, Pensato S, Pedone C, Iannelli D
* Synergistic antibacterial and anti-inflammatory activity of temporin A and modified temporin B in vivo (115 visite)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 28; 4(9): e7191-e7191.
Impact Factor: 4.351
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Palladino P, Ronga L, Benedetti E, Rossi F, Ragone R
* Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (130 visite)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
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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 (103 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009; 15(1): 30-35.
Impact Factor: 1.807
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Giuffrida M, Caraci F, Molinaro G, Cataldo S, Pignataro B, Bruno V, De Bona P, Pappalardo G, Messina A, Palmigiano A, Garozzo D, Nicoletti F, Rizzarelli E, Copani AG
* Monomers of beta-amyloid protein are endowed with neuroprotective activity (120 visite)
Society For Neuroscience Abstract Viewer And Itinerary Planner, 2009; 39: N/D-N/D.
Impact Factor: 0
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La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion proteins leading to neurodegeneration (143 visite)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
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Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (141 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
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Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R, Rossi F
* Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides (156 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
Impact Factor: 1.654
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Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M
* Does Tetracycline Bind Helix 2 Of Prion? An Integrated Spectroscopical And Computational Study Of The Interaction Between The Antibiotic And Alpha Helix 2 Human Prion Protein Fragments (166 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Feb 15; 66(3): 707-715.
Impact Factor: 3.354
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Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
* Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (146 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
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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 (146 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
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Agmon I, Amit M, Auerbach T, Bashan A, Baram D, Bartels H, Berisio R, Greenberg I, Harms J, Hansen HAS, Kessler M, Pyetan E, Schluenzen F, Sittner A, Yonath A, Zarivach R
* Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (85 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (148 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
* Structural insight into the role of the ribosomal tunnel in cellular regulation (103 visite)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
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Wiesehan K, Buder K, Linke RP, Patt S, Stoldt M, Unger E, Schmitt B, Bucci E, Willbold D
* Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide Aβ1-42 by mirror image phage display (181 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2003; 4(8): 748-753.
Impact Factor: 3.992
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Monti SM, Fogliano V, Logrieco A, Ferracane R, Ritieni A
Simultaneous determination of beauvericin, enniatins, and fusaproliferin by high performance liquid chromatography (151 visite)
J Agric Food Chem (ISSN: 0021-8561), 2000 Sep; 48(8): 3317-3320.
Impact Factor: 1.56
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38 Records (35 escludendo Abstract e Conferenze).
Impact factor totale: 122.536 (116.409 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 127.338 (120.992 escludendo Abstract e Conferenze).







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