Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (741 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
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Paper type: Journal Article,
Impact factor: 1.801, 5-year impact factor: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845662273&partnerID=40&md5=c91b9da830e9a36bb0f540ad5eb00a1a
Keywords: Amyloid, Anions, Cations, Counterions, Hofmeister Series, Prion Helix 2 Derived Peptides, Prion Structure, Transmissible Spongiform Encephalopathies, Prion Protein, Prion Protein Helix 2 Derivative, Sodium Chloride, Alpha Helix, Article, Beta Sheet, Human, Ionic Strength, Peptide Synthesis, Priority Journal, Protein Binding, Protein Conformation, Protein Folding, Protein Function, Protein Modification, Amino Acid Sequence, Circular Dichroism, Electrostatics, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Salts, Sulfates,
Affiliations:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, C.I.R.Pe.B, Università Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
References:
Not available.
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.801, 5-year impact factor: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845662273&partnerID=40&md5=c91b9da830e9a36bb0f540ad5eb00a1a
Keywords: Amyloid, Anions, Cations, Counterions, Hofmeister Series, Prion Helix 2 Derived Peptides, Prion Structure, Transmissible Spongiform Encephalopathies, Prion Protein, Prion Protein Helix 2 Derivative, Sodium Chloride, Alpha Helix, Article, Beta Sheet, Human, Ionic Strength, Peptide Synthesis, Priority Journal, Protein Binding, Protein Conformation, Protein Folding, Protein Function, Protein Modification, Amino Acid Sequence, Circular Dichroism, Electrostatics, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Salts, Sulfates,
Affiliations:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, C.I.R.Pe.B, Università Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
References:
Not available.
Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective
Both theoretical studies and direct experimental evidence have emphasized the importance of electrostatic interactions in the general phenomenon of spontaneous amyloid fibril formation. A number of observations have recently spurred interest in the contribution of these interactions to the conformational behavior of the prion protein. In this paper, we show how salt addition and pH change can modify the conformation of two peptide analogues derived from the human prion protein helix 2 according to a Hofmeister-series-type dependence. Employment of various sodium salts allowed us to highlight the fact that chaotropic anions favor unstructured conformation, whereas kosmotropic anions promote the formation of compact structures like α-helix and β-sheet, which may ultimately facilitate fibril formation. This finding should warn people engaged in ion-based research on prion and derived peptides about cation-bound effects, which have been almost exclusively investigated to date, being easily confounded with modifications that are actually caused by anion activity, thus leading researchers into misunderstand ion-specific effects. To avoid the common complication of ion confounding, it is highly desirable that experiments be designed so that the species causing the modification can be unequivocally perceived. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.
Both theoretical studies and direct experimental evidence have emphasized the importance of electrostatic interactions in the general phenomenon of spontaneous amyloid fibril formation. A number of observations have recently spurred interest in the contribution of these interactions to the conformational behavior of the prion protein. In this paper, we show how salt addition and pH change can modify the conformation of two peptide analogues derived from the human prion protein helix 2 according to a Hofmeister-series-type dependence. Employment of various sodium salts allowed us to highlight the fact that chaotropic anions favor unstructured conformation, whereas kosmotropic anions promote the formation of compact structures like α-helix and β-sheet, which may ultimately facilitate fibril formation. This finding should warn people engaged in ion-based research on prion and derived peptides about cation-bound effects, which have been almost exclusively investigated to date, being easily confounded with modifications that are actually caused by anion activity, thus leading researchers into misunderstand ion-specific effects. To avoid the common complication of ion confounding, it is highly desirable that experiments be designed so that the species causing the modification can be unequivocally perceived. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.
Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective
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Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective
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* Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (727 views)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
View Export to BibTeX Export to EndNote
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 (476 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009; 15(1): 30-35.
Impact Factor: 1.807
View Export to BibTeX Export to EndNote
Ronga L, Palladino P, Costantini S, Facchiano A, Ruvo M, Benedetti E, Ragone R, Rossi F
* Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (1064 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
View Export to BibTeX Export to EndNote
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 (851 views)
Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285), 2006 Sep; 68(3): 139-147.
Impact Factor: 2.507
View Export to BibTeX Export to EndNote
4 Records (4 excluding Abstracts).
Total impact factor: 8.442 (8.442 excluding Abstracts).
Total 5 year impact factor: 8.969 (8.969 excluding Abstracts).
Total impact factor: 8.442 (8.442 excluding Abstracts).
Total 5 year impact factor: 8.969 (8.969 excluding Abstracts).
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