Open AccessNMR 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
Author(s) -
Riek Roland,
Güntert Peter,
Döbeli Heinz,
Wipf Beat,
Wüthrich Kurt
Publication year - 2001
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.0014-2956.2001.02537.x
Subject(s) - random coil , aqueous solution , chemistry , amyloid beta , monomer , peptide , peptide sequence , globular protein , stereochemistry , methionine sulfoxide , beta (programming language) , molecule , crystallography , amino acid , methionine , circular dichroism , biochemistry , polymer , organic chemistry , gene , computer science , programming language
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) ox or Aβ(1–42) ox (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) ox and Aβ(1–42) ox are indicated only by decreased flexibility of the region from about residue 32 to the C‐terminus in Aβ(1–42) ox when compared to Aβ(1–40) ox . The lack of the observation of more extensive conformational differences between the two molecules is intriguing, considering that Aβ(1–42) ox in aqueous solution has much higher plaque‐competence than Aβ(1–40) ox .