A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix
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A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix
(
394 views
)
Ronga L, Palladino P, Ragone R, Benedetti E,
Rossi F
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print)
,
2009;
15(1): 30-35.
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Paper type:
Journal Article,
Impact factor:
1.807,
5-year impact factor:
1.872
Url:
http://www.scopus.com/inward/record.url?eid=2-s2.0-61749083187&partnerID=40&md5=8210b7cb614a6a772db689e99a40f328
Keywords:
α2-Helix, β-Sheet, Amyloid, Cd Titration, Prion Protein, Prion Toxicity, Structure-Inducing Agents, Transmissible Spongiform Encephalopathies, Alanine, Alpha Helix, Amino Acid Substitution, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Circular Dichroism, Conformational Transition, Controlled Study, Priority Journal, Protein Conformation, Protein Stability, Protein Structure, Quantitative Analysis, Thermodynamics, Wild Type, Amino Acid Sequence, Humans, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Secondary, Tertiary,
Affiliations:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, C.I.R.Pe.B., Università Federico II di Napoli, Via Mezzocannone 16, Naples 80134, Italy
References:
Not available.
A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix
On consideration that intrinsic structural weakness could affect the segment spanning the α2-helical residues 173-195 of the PrP, we have investigated the conformational stabilities of some synthetic Ala-scanned analogs of the peptide derived from the 180-195 C-terminal sequence, using a novel approach whose theoretical basis originates from protein thermodynamics. Even though a quantitative comparison among peptides could not be assessed to rank them according to the effect caused by single amino acid substitution, as a general trend, all peptides invariably showed an appreciable preference for an α-type organization, consistently with the fact that the wild-type sequence is organized as an α-helix in the native protein. Moreover, the substitution of whatever single amino acid in the wild-type sequence reduced the gap between the α- and the β-propensity, invariably enhancing the latter, but in any case this gap was larger than that evaluated for the full-length α2-helix-derived peptide. It appears that the low β-conformation propensity of the 180-195 region depends on the simultaneous presence of all of the Ala-scanned residues, indirectly confirming that the N-terminal 173-179 segment could play a major role in determining the chameleon conformational behavior of the entire 173-195 region in the PrP. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.
A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix
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A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix
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Di Natale C, La Manna S, Avitabile C, Florio D,
Morelli G
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Marasco D
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De Simonea A, Stanzione F,
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Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R,
Rossi F
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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
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Ronga L,
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Ronga L, Palladino P, Costantini S, Facchiano A,
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Rao M, Russo F, Granata V,
Berisio R
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Osz K, Nagy Z, Pappalardo G, Di Natale G, Sanna D, Micera G, Rizzarelli E, Sóvágó I
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Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details
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Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R,
Rossi F
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NMR structure and CD titration with metal cations of human prion α2-helix-related peptides
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Pappalardo M, Milardi D, Grasso D, La Rosa C
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Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species
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Ronga L, Palladino P, Tizzano B,
Marasco D
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Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective
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Esposito L
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Pedone C
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Vitagliano L
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Ronga L, Tizzano B, Palladino P, Ragone R, Urso E, Maffia M,
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Joszal V, Nagy Z, Osz K, Sanna D, Di Natale G, La Mendola D, Pappalardo G, Rizzarelli E, Sovago I
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Transition metal complexes of terminally protected peptides containing histidyl residues
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Langella E
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Improta R
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Palladino P, Ronga L, Tizzano B,
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Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
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La Mendola D, Bonomo RP, Impellizzeri G, Maccarrone G, Pappalardo G, Pietropaolo A, Rizzarelli E, Zito V
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Copper(II) complexes with chicken prion repeats: Influence of proline and tyrosine residues on the coordination features
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Tizzano B, Palladino P, De Capua A,
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Di Natale G, Impellizzeri G, Pappalardo G
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Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study
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Bonomo RP, Cucinotta V, Giuffrida A, Impellizzeri G, Magrì A, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
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Langella E
,
Improta R
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Checking the pH-induced conformational transition of prion protein by molecular dynamics simulations: Effect of protonation of histidine residues
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Pappalardo M, Milardi D, La Rosa C, Zannoni C, Rizzarelli E, Grasso D
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A molecular dynamics study on the conformational stability of PrP 180-193 helix II prion fragment
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774 views
)
Chem Phys Lett (ISSN: 0009-2614)
,
2004 Jun 1;
390(4-6): 511-516.
Impact Factor:
2.438
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
*
The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes
(
399 views
)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic)
,
2004 Jan 21;
10(2): 246-247.
Impact Factor:
3.997
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Brown DR, 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
(
813 views
)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print)
,
2004 Jan;
98(1): 133-143.
Impact Factor:
2.225
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Barone V,
Improta R
, Rega N
*
Computation of protein pK's values by an integrated density functional theory/Polarizable Continuum Model approach
(
418 views
)
Theor Chem Acc (ISSN: 1432-881x)
,
2004;
111(2-6): 237-245.
Impact Factor:
2.209
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Tizzano B,
Marasco D
, Benedetti E, De Capua A, Palladino P,
Pedone C
, Perretta G,
Rossi F
, Ragone R,
Ruvo M
*
Conformational conversion of prion proteins: Role synthetic PRP 173-195 fibrillogenic peptide
(
446 views
)
Peptide Revolution
,
2004;
N/D: N/D-N/D.
Impact Factor:
4.659
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Pappalardo G, Impellizzeri G, Campagna T
*
Copper(II) binding of prion protein's octarepeat model peptides
(
668 views
)
Inorg Chim Acta (ISSN: 0020-1693)
,
2004;
357(1): 185-194.
Impact Factor:
1.554
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La Mendola D, Bonomo R, Maccarrone G, Pappalardo G, Rizzarelli E
*
A thermodynamic and spectroscopic study on the copper(II) complexes with hexarepeats fragments of the avian prion protein
(
468 views
)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print)
,
2003 Jul 15;
96(1): N/D-N/D.
Impact Factor:
2.343
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Bonomo RP, Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Pappalardo G, Tabbì G, Rizzarelli E
*
Metal binding to prion protein
(
337 views
)
Metal-Ligand Interactions - Molecular Nano- Micro- And Macro-Systems In Complex Environments
,
2003 Jan 01;
116: 21-39.
Impact Factor:
5.664
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Grasso D, Milardi D, Guantieri V, La Rosa C, Rizzarelli E
*
Interaction of prion peptide PrP 180-193 with DPPC model membranes: A thermodynamic study
(
614 views
)
New J Chem (ISSN: 1144-0546)
,
2003;
27(2): 359-364.
Impact Factor:
2.272
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Menziani MC, De Benedetti PG,
Langella E
, Barone V
*
Seeking for binding determinants of the prion protein to human plasminogen
(
570 views
)
Mol Phys (ISSN: 0026-8976)
,
2003;
101(17): 2763-2773.
Impact Factor:
1.591
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
*
DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes
(
441 views
)
New J Chem (ISSN: 1144-0546)
,
2001;
25(12): 1543-1548.
Impact Factor:
2.44
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Bonomo RP, Imperllizzeri G, Pappalardo G, Rizzarelli E, Tabbì G
Copper(II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study
(
594 views
)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic)
,
2000 Nov 17;
6(22): 4195-4202.
Impact Factor:
4.698
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59
Records (
52
excluding Abstracts).
Total impact factor:
198.479
(
177.596
excluding Abstracts).
Total 5 year impact factor:
209.855
(
186.998
excluding Abstracts).
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