Control of the toxic conformation of amyloid β42 by intramolecular disulfide bond formation

We report a method to fix the conformation of A beta 42 to the toxic or non-toxic form by intramolecular disulfide bonds. We found that an A beta 42 analog crosslinked within the molecule at the 17th and 28th amino acid residues exhibited high aggregative ability and potent neurotoxicity comparable to those of E22P-A beta 42. This analog would be useful in the research of A beta 42 oligomers and to develop reliable antibodies for early diagnosis of Alzheimer's disease.