[NMR paper] 3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol ?-viniferin glucoside: implications in Alzheimer's disease.
Related Articles3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol ?-viniferin glucoside: implications in Alzheimer's disease.
Biochim Biophys Acta. 2013 Nov;1830(11):5068-74
Authors: Richard T, Papastamoulis Y, Waffo-Teguo P, Monti JP
Abstract
BACKGROUND: Alzheimer's disease (AD) is a progressive neurodegenerative disorder. There is a consensus that A? is a pathologic agent and that its toxic effects, which are at present incompletely understood, may occur through several potential mechanisms. Polyphenols are known to have wide-ranging properties with regard to health and for helping to prevent various diseases like neurodegenerative disorders. Thus inhibiting the formation of toxic A? assemblies is a reasonable hypothesis to prevent and perhaps treat AD METHODS: Solution NMR and molecular modeling were used to obtain more information about the interaction between the A?1-40 and the polyphenol ?-viniferin glucoside (EVG) and particularly the A? residues involved in the complex.
RESULTS: The study demonstrates the formation of a complex between two EVG molecules and A?1-40 in peptide characteristic regions that could be in agreement with the inhibition of aggregation. Indeed, in previous studies, we reported that EVG strongly inhibited in vitro the fibril formation of the full length peptides A?1-40 and A?1-42, and had a strong protective effect against PC12 cell death induced by these peptides.
CONCLUSION: For the full length peptide A?1-40, the binding sites observed could explain the EVG inhibitory effect on fibrillization and thus prevent amyloidogenic neurotoxicity.
GENERAL SIGNIFICANCE: Even though this interaction might be important at the biological level to explain the protective effect of polyphenols in neurodegenerative diseases, caution is required when extrapolating this in vitro model to human physiology.
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
From The DNP-NMR Blog:
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
Lopez Del Amo, J.M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP. J Biomol NMR, 2013: p. 1-5.
http://www.ncbi.nlm.nih.gov/pubmed/23793606
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Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
From The DNP-NMR Blog:
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
Lopez del Amo, J.-M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-? peptide: perspectives for DNP. J. Biomol. NMR, 2013: p. 1-5.
http://www.ncbi.nlm.nih.gov/pubmed/23793606
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07-19-2013 09:20 PM
[NMR paper] Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Molecules. 2013;18(5):4929-41
Authors: Ramírez-Gualito K, Richter M, Matzapetakis M, Singer D, Berger S
Abstract
Rational design of peptide vaccines becomes important for the treatment of some diseases such as Alzheimer's disease (AD) and related disorders. In this study, as part of a larger...
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04-30-2013 10:21 PM
[NMR paper] Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-? using NMR spectroscopy.
Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-? using NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Structural analysis of the pyroglutamate-modified isoform of the Alzheimer's disease-related amyloid-? using NMR spectroscopy.
J Pept Sci. 2012 Nov;18(11):691-5
Authors: Sun N, Hartmann R, Lecher J, Stoldt M, Funke SA, Gremer L, Ludwig HH, Demuth HU, Kleinschmidt M,...
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[NMR paper] Expression and purification of a recombinant peptide from the Alzheimer's beta-amyloi
Expression and purification of a recombinant peptide from the Alzheimer's beta-amyloid protein for solid-state NMR.
Related Articles Expression and purification of a recombinant peptide from the Alzheimer's beta-amyloid protein for solid-state NMR.
Protein Expr Purif. 2005 Jul;42(1):200-10
Authors: Sharpe S, Yau WM, Tycko R
Fibrillar protein aggregates contribute to the pathology of a number of disease states. To facilitate structural studies of these amyloid fibrils by solid-state NMR, efficient methods for the production of milligram...
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11-24-2010 11:14 PM
[NMR paper] Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's
Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.
Related Articles Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.
Biochemistry. 2000 Nov 14;39(45):13748-59
Authors: Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH(2), called A...
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[NMR paper] An unusual peptide conformation may precipitate amyloid formation in Alzheimer's dise
An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.
Related Articles An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.
Biochemistry. 1991 Oct 29;30(43):10382-7
Authors: Spencer RG, Halverson KJ, Auger M, McDermott AE, Griffin RG, Lansbury PT
The formation of insoluble proteinaceous deposits is...
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08-21-2010 11:12 PM
[NMR paper] An unusual peptide conformation may precipitate amyloid formation in Alzheimer's dise
An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.
Related Articles An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.
Biochemistry. 1991 Oct 29;30(43):10382-7
Authors: Spencer RG, Halverson KJ, Auger M, McDermott AE, Griffin RG, Lansbury PT
The formation of insoluble proteinaceous deposits is...