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The solvent protection of alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy.
Umeå universitet, Medicinska fakulteten, Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten). (Sauer-Eriksson)
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet).
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
2006 (Engelska)Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, Vol. 281, nr 1, s. 477-83Artikel i tidskrift (Refereegranskat) Published
Fritextbeskrivning
Abstract [en]

Alzheimer disease is a neurodegenerative disorder that is tightly linked to the self-assembly and amyloid formation of the 39-43-residue-long amyloid-beta (Abeta) peptide. Considerable evidence suggests a correlation between Alzheimer disease development and the longer variants of the peptide, Abeta-(1-42/43). Currently, a molecular understanding for this behavior is lacking. In the present study, we have investigated the hydrogen/deuterium exchange of Abeta-(1-42) fibrils under physiological conditions, using solution NMR spectroscopy. The obtained residue-specific and quantitative map of the solvent protection within the Abeta-(1-42) fibril shows that there are two protected core regions, Glu11-Gly25 and Lys28-Ala42, and that the residues in between, Ser26 and Asn27, as well as those in the N terminus, Asp1-Tyr10, are solvent-accessible. This result reveals considerable discrepancies when compared with a previous investigation on Abeta-(1-40) fibrils and suggests that the additional residues in Abeta-(1-42), Ile41 and Ala42, significantly increase the solvent protection and stability of the C-terminal region Lys28-Ala42. Consequently, our findings provide a molecular explanation for the increased amyloidogenicity and toxicity of Abeta-(1-42) compared with shorter Abeta variants found in vivo.

Ort, förlag, år, upplaga, sidor
2006. Vol. 281, nr 1, s. 477-83
Nyckelord [en]
Amyloid/*chemistry, Amyloid beta-Protein/*chemistry, Deuterium Exchange Measurement, Humans, Microscopy; Atomic Force, Nuclear Magnetic Resonance; Biomolecular, Peptide Fragments/*chemistry, Solubility, Solvents
Identifikatorer
URN: urn:nbn:se:umu:diva-13607DOI: doi:10.1074/jbc.M508962200PubMedID: 16215229OAI: oai:DiVA.org:umu-13607DiVA, id: diva2:153278
Tillgänglig från: 2008-04-08 Skapad: 2008-04-08 Senast uppdaterad: 2018-06-09Bibliografiskt granskad

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Olofsson, AndersSauer-Eriksson, ElisabethÖhman, Anders

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Olofsson, AndersSauer-Eriksson, ElisabethÖhman, Anders
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Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten)Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)Kemiska institutionen

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