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High-resolution NMR studies of the sinc-binding site of the Alzheimer’s Aβ-peptide
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.ORCID-id: 0000-0002-6048-6896
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
2007 (Engelska)Ingår i: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 274, nr 1, s. 46-59Artikel i tidskrift (Refereegranskat) Published
Ort, förlag, år, upplaga, sidor
2007. Vol. 274, nr 1, s. 46-59
Identifikatorer
URN: urn:nbn:se:su:diva-23079DOI: 10.1111/j.1742-4658.2006.05563.xISI: 000242782600004OAI: oai:DiVA.org:su-23079DiVA, id: diva2:190045
Anmärkning
Part of urn:nbn:se:su:diva-1410Tillgänglig från: 2007-01-02 Skapad: 2007-01-02 Senast uppdaterad: 2022-02-25Bibliografiskt granskad
Ingår i avhandling
1. NMR studies of the amyloid beta-peptide
Öppna denna publikation i ny flik eller fönster >>NMR studies of the amyloid beta-peptide
2007 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

The Amyloid beta peptide (Ab) is related to Alzheimer’s disease and is suggested to be the molecular pathogenic species of the disease, probably through the neurotoxic effect of Ab oligomers. Here the results from biophysical studies of Ab and fragments thereof, are presented. Pulsed field gradient NMR diffusion experiments show that Ab exists mainly as an unfolded monomer. In addition, the hydrodynamic radius of Ab suggests that Ab has residual secondary structure propensities. CD experiments reveal that Ab has a high propensity to adopt a polyproline type II (PII) helix at low temperature. NMR diffusion measurements as well as the 3JHNH values show that increasing the temperature from 4 C induces a structure transition from PII propensity to a beta strand propensity around 15 C and to a random coil conformation at higher temperature. The small hydrodynamic radius at low temperature may be explained by the presence of a population of a hairpin conformation as was suggested by MD simulations. 15N relaxation and secondary chemical shifts suggest that Ab consists of 6 structural regions, two regions with high PII propensity are separated by a highly mobile region located in the N-terminal part of the peptide. In the C-terminal part two regions with a propensity to adopt b-strand are located, separated by a mobile region. The structural propensities of soluble monomeric Ab agree well with the structure of the peptide in fibril aggregates as well as in SDS micelles. Ab binds zinc specifically and with high affinity. This interaction was studied using heteronuclear correlation experiments. The metal ligands were determined to be three histidines, 6,13 and 14 and the N-terminus. The Ab peptide also binds b-cyclodextrin and the combined use of NMR diffusion experiments and induced chemical shifts show that Ab has at least two binding sites for b-cyclodextrin, and the dissociation constants of these binding sites were determined.

Ort, förlag, år, upplaga, sidor
Stockholm: Institutionen för biokemi och biofysik, 2007. s. 86
Nyckelord
NMR, amyloid beta peptide, structure, metal interaction, diffusion
Nationell ämneskategori
Biofysik
Identifikatorer
urn:nbn:se:su:diva-1410 (URN)91-7155-349-5 (ISBN)
Disputation
2007-01-26, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00
Opponent
Handledare
Tillgänglig från: 2007-01-02 Skapad: 2007-01-02Bibliografiskt granskad

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Danielsson, JensGräslund, Astrid

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The FEBS Journal

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Totalt: 61 träffar
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