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Search: onr:"swepub:oai:DiVA.org:umu-13597" > Amide solvent prote...

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  • Olofsson, AndersUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten) (author)

Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions.

  • Article/chapterEnglish2007

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  • 2007
  • printrdacarrier

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  • LIBRIS-ID:oai:DiVA.org:umu-13597
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-13597URI

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  • Language:English
  • Summary in:English &language:-1_t

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

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  • AD (Alzheimer's disease) is a neurodegenerative disorder characterized by self-assembly and amyloid formation of the 39–43 residue long Ab (amyloid-b)-peptide. The most abundant species, Ab(1–40) and Ab(1–42), are both present within senile plaques, but Ab(1–42) peptides are considerably more prone to self-aggregation and are also essential for the development of AD. To understand the molecular and pathological mechanisms behind AD, a detailed knowledge of the amyloid structures of Ab-peptides is vital. In the present study we have used quenched hydrogen/deuterium-exchange NMR experiments to probe the structure of Ab(1–40) fibrils. The fibrils were prepared and analysed identically as in our previous study on Ab(1–42) fibrils, allowing a direct comparison of the two fibrillar structures. The solvent protection pattern of Ab(1–40) fibrils revealed two well-protected regions, consistent with a structural arrangement of two b-strands connected with a bend. This protection pattern partly resembles the pattern found in Ab(1–42) fibrils, but the Ab(1–40) fibrils display a significantly increased protection for the N-terminal residues Phe4–His14, suggesting that additional secondary structure is formed in this region. In contrast, the C-terminal residues Gly37–Val40 show a reduced protection that suggests a loss of secondary structure in this region and an altered filament assembly. The differences between the present study and other similar investigations suggest that subtle variations in fibril-preparation conditions may significantly affect the fibrillar architecture.

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  • Lindhagen-Persson, MalinUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet) (author)
  • Sauer-Eriksson, ElisabethUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)(Swepub:umu)elsa0002 (author)
  • Öhman, AndersUmeå universitet,Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)(Swepub:umu)anoh0004 (author)
  • Umeå universitetUmeå centrum för molekylär patogenes (UCMP) (Medicinska fakulteten) (creator_code:org_t)

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  • In:Biochem J404:1, s. 63-701470-8728

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Olofsson, Anders
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Öhman, Anders
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NATURAL SCIENCES
NATURAL SCIENCES
and Biological Scien ...
and Structural Biolo ...
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Biochem J
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Umeå University

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