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1: Eur J Biochem 2001 Nov;268(22):5930-6

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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, Abeta(1-40)ox and Abeta(1-42)ox.

Riek R, Guntert P, Dobeli H, Wipf B, Wuthrich K.

Institut fur Molekularbiolgie und Biophysik, Eidgenossische Technische Hochschule-Honggerberg, Zurich, Switzerland; Hoffmann-La Roche Ltd, Basel, Switzerland.

NMR studies of amyloid beta-peptides (Abeta) in aqueous solution provide a novel way in which to characterize the apparent Alzheimer's disease-related conformational polymorphism of Abeta. In the aqueous medium, neither of the polypeptides Abeta(1-40)ox or Abeta(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 Abeta(1-40)ox and Abeta(1-42)ox are indicated only by decreased flexibility of the region from about residue 32 to the C-terminus in Abeta(1-42)ox when compared to Abeta(1-40)ox. The lack of the observation of more extensive conformational differences between the two molecules is intriguing, considering that Abeta(1-42)ox in aqueous solution has much higher plaque-competence than Abeta(1-40)ox.

PMID: 11722581 [PubMed - in process]

sparc-sun-solaris2.8 Nov 15 2001 10:41:10