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 (504 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
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Paper type: Journal Article,
Impact factor: 2.547, 5-year impact factor: 3.389
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-14244269453&partnerID=40&md5=49d4944503d74987c90e24813a2a6161
Keywords: Amyloidogenic Peptide Fragment, Fatal Familial Insomnia (ffi), Human Prion Proteins, Neurotoxic Effect, Conformations, Electrostatics, Hydrophobicity, Ionic Strength, Micelles, Nuclear Magnetic Resonance, Ph Effects, Article, Chemistry, Circular Dichroism, Methodology, Nuclear Magnetic Resonance Spectroscopy, Protein Conformation, Protein Secondary Structure, Sensitivity And Specificity, Protein Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 95125, Catania, Italy
Istituto di Biostrutture, Bioimmagini-Sezione di Catania, CNR, V.le A. Doria 6, 95125, Catania, Italy
References:
Not available.
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.547, 5-year impact factor: 3.389
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-14244269453&partnerID=40&md5=49d4944503d74987c90e24813a2a6161
Keywords: Amyloidogenic Peptide Fragment, Fatal Familial Insomnia (ffi), Human Prion Proteins, Neurotoxic Effect, Conformations, Electrostatics, Hydrophobicity, Ionic Strength, Micelles, Nuclear Magnetic Resonance, Ph Effects, Article, Chemistry, Circular Dichroism, Methodology, Nuclear Magnetic Resonance Spectroscopy, Protein Conformation, Protein Secondary Structure, Sensitivity And Specificity, Protein Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università di Catania, V.le A. Doria 6, 95125, Catania, Italy
Istituto di Biostrutture, Bioimmagini-Sezione di Catania, CNR, V.le A. Doria 6, 95125, Catania, Italy
References:
Not available.
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
Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP[Ac-106-126-NH2]) and 106-114 (PrP[Ac-106-114-NH2]) of the human prion protein have been synthesised in the acetylated and amide form at their N- and C-termini, respectively. The conformational preferences of PrP[Ac-106-126-NH2] and PrP[Ac-106-114-NH2] were investigated using CD and NMR spectroscopy. CD results showed that PrP[Ac-106-126-NH2] mainly adopts an alpha-helical conformation in TFE water mixture and in SDS micelles, while a predominantly random structure is observed in aqueous solution. The shorter PrP[Ac-106-114-NH2] fragment showed similar propensities when investigated under the same experimental conditions as those employed for PrP[Ac-106-126-NH2]. From CD experiments at different SDS concentrations, an alpha-helix/beta-sheet conformational transition was only observed in the blocked PrP[Ac-106-126-NH2] sequence. The NMR analysis confirmed the helical nature of PrP[Ac-106-126-NH2] in the presence of SDS micelles. The shorter PrP[Ac-106-114-NH2] manifested a similar behaviour. The results as a whole suggest that both hydrophobic effects and electrostatic interactions play a significant role in the formation and stabilisation of ordered secondary structures in PrP [Ac-106-126-NH2].
Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP[Ac-106-126-NH2]) and 106-114 (PrP[Ac-106-114-NH2]) of the human prion protein have been synthesised in the acetylated and amide form at their N- and C-termini, respectively. The conformational preferences of PrP[Ac-106-126-NH2] and PrP[Ac-106-114-NH2] were investigated using CD and NMR spectroscopy. CD results showed that PrP[Ac-106-126-NH2] mainly adopts an alpha-helical conformation in TFE water mixture and in SDS micelles, while a predominantly random structure is observed in aqueous solution. The shorter PrP[Ac-106-114-NH2] fragment showed similar propensities when investigated under the same experimental conditions as those employed for PrP[Ac-106-126-NH2]. From CD experiments at different SDS concentrations, an alpha-helix/beta-sheet conformational transition was only observed in the blocked PrP[Ac-106-126-NH2] sequence. The NMR analysis confirmed the helical nature of PrP[Ac-106-126-NH2] in the presence of SDS micelles. The shorter PrP[Ac-106-114-NH2] manifested a similar behaviour. The results as a whole suggest that both hydrophobic effects and electrostatic interactions play a significant role in the formation and stabilisation of ordered secondary structures in PrP [Ac-106-126-NH2].
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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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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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Proc Electrochem Soc, 2004; 10: 29-32.
Impact Factor: 0
View Export to BibTeX Export to EndNote
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Impact Factor: 3.922
View Export to BibTeX Export to EndNote
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Impact Factor: 4.353
View Export to BibTeX Export to EndNote
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Impact Factor: 3.621
View Export to BibTeX Export to EndNote
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Impact Factor: 2.792
View Export to BibTeX Export to EndNote
Bonomo RP, Bruno V, Conte E, De Guidi G, La Mendola D, Maccarrone G, Nicoletti F, Rizzarelli E, Sortino S, Vecchio G
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Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2003; (23): 4406-4415.
Impact Factor: 2.908
View Export to BibTeX Export to EndNote
Zanotti G, Falcigno L, Saviano M, D'Auria G, Bruno BM, Campanile T, Paolillo L
* Solid state and solution conformation of [Ala7]-phalloidin: A synthetic phallotoxin analogue (593 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2001; 7(7): 1479-1485.
Impact Factor: 4.614
View Export to BibTeX Export to EndNote
Crisma M, Formaggio F, Valle G, Toniolo C, Saviano M, Iacovino R, Zaccaro L, Benedetti E
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1997; 42(1): 1-6.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Lombardi A, Saviano M, Nastri F, Maglio O, Mazzeo M, Pedone C, Isernia C, Pavone V
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1996 Jun; 38(6): 683-691.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Bustamante C, Gurrieri S, Pasternack RF, Purrello R, Rizzarelli E
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Sep; 34(8): 1099-1104.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Tancredi T, Zanotti G, Rossi F, Benedetti E, Pedone C, Temussi PA
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1989 Jan; 28(1): 513-523.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
Capasso S, Mazzarella L, Sica F, Zagari A
Solid-state conformations of aminosuccinyl peptides: crystal structure of tert-butyloxycarbonyl-L-leucyl-L-aminosuccinyl-L-phenylalaninami de (739 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1989; 28(1): 139-147.
Impact Factor: 2.425
View Export to BibTeX Export to EndNote
22 Records (22 excluding Abstracts).
Total impact factor: 74.589 (74.589 excluding Abstracts).
Total 5 year impact factor: 86.133 (86.133 excluding Abstracts).
Total impact factor: 74.589 (74.589 excluding Abstracts).
Total 5 year impact factor: 86.133 (86.133 excluding Abstracts).
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