Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer's amyloid Aβ10-35 peptide in solution and in SDS micelles

The spatial structure of Alzheimer's amyloid A beta(10-35)-NH2 peptide in aqueous solution at pH 7.3 and in SDS micelles was investigated by use of a combination of the residual dipolar coupling method and two-dimensional NMR spectroscopy (TOCSY, NOESY). At pH 7.3 A beta(10-35)-NH2 adopts a compact random-coil conformation whereas in SDS micellar solutions two helical regions (residues 13-23 and 30-35) of A beta(10-35)-NH2 were observed. By use of experimental data, the structure of peptide-micelle complex was determined; it was found that A beta(10-35)-NH2 peptide binds to the micelle surface at two regions (residues 17-20 and 29-35).