Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization

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Abstract
Aβ40 and Aβ42 are peptides that adopt similar random-coil structures in solution. Aβ42, however, is significantly more neurotoxic than Aβ40 and forms amyloid fibrils much more rapidly than Aβ40. Here, mass spectrometry and ion mobility spectrometry are used to investigate a mixture of Aβ40 and Aβ42. The mass spectrum for the mixed solution shows the presence of a heterooligomer composed of equal parts of Aβ40 and Aβ42. Ion mobility results indicate that this mixed species comprises an oligomer distribution extending to tetramers. Aβ40 alone produces such a distribution, whereas Aβ42 alone produces oligomers as large as dodecamers. This indicates that Aβ40 inhibits Aβ42 oligomerization.