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NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)ox and Aβ(1–42)ox.
- Source :
- European Journal of Biochemistry; Nov2001, Vol. 268 Issue 22, p5930-5936, 7p, 1 Chart, 4 Graphs
- Publication Year :
- 2001
-
Abstract
- NMR studies of amyloid β-peptides (Aβ) in aqueous solution provide a novel way in which to characterize the apparent Alzheimer’s disease-related conformational polymorphism of Aβ. In the aqueous medium, neither of the polypeptides Aβ(1–40)<superscript>ox</superscript> or Aβ(1–42)<superscript>ox</superscript> (both of which contain a methionine sulfoxide at position 35) is folded into a globular structure, but they both deviate from random coil behavior by local conformational preferences of several short segments along the amino-acid sequence. Differences between the solution structures of Aβ(1–40)<superscript>ox</superscript> and Aβ(1–42)<superscript>ox</superscript> are indicated only by decreased flexibility of the region from about residue 32 to the C-terminus in Aβ(1–42)<superscript>ox</superscript> when compared to Aβ(1–40)<superscript>ox</superscript>. The lack of the observation of more extensive conformational differences between the two molecules is intriguing, considering that Aβ(1–42)<superscript>ox</superscript> in aqueous solution has much higher plaque-competence than Aβ(1–40)<superscript>ox</superscript>. [ABSTRACT FROM AUTHOR]
- Subjects :
- PEPTIDES
ALZHEIMER'S disease
MONOMERS
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 268
- Issue :
- 22
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 6031699
- Full Text :
- https://doi.org/10.1046/j.0014-2956.2001.02537.x