Murray Megan M, Bernstein Summer L, Nyugen Vy, Condron Margaret M, Teplow David B, Bowers Michael T
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106-950, USA.
J Am Chem Soc. 2009 May 13;131(18):6316-7. doi: 10.1021/ja8092604.
Abeta40 and Abeta42 are peptides that adopt similar random-coil structures in solution. Abeta42, however, is significantly more neurotoxic than Abeta40 and forms amyloid fibrils much more rapidly than Abeta40. Here, mass spectrometry and ion mobility spectrometry are used to investigate a mixture of Abeta40 and Abeta42. The mass spectrum for the mixed solution shows the presence of a heterooligomer composed of equal parts of Abeta40 and Abeta42. Ion mobility results indicate that this mixed species comprises an oligomer distribution extending to tetramers. Abeta40 alone produces such a distribution, whereas Abeta42 alone produces oligomers as large as dodecamers. This indicates that Abeta40 inhibits Abeta42 oligomerization.
β淀粉样蛋白40(Aβ40)和β淀粉样蛋白42(Aβ42)是在溶液中具有相似无规卷曲结构的肽段。然而,Aβ42比Aβ40具有显著更强的神经毒性,并且比Aβ40更快地形成淀粉样纤维。在此,采用质谱和离子淌度谱来研究Aβ40和Aβ42的混合物。混合溶液的质谱显示存在由等量的Aβ40和Aβ42组成的异源寡聚体。离子淌度结果表明这种混合物种包含延伸至四聚体的寡聚体分布。单独的Aβ40产生这样的分布,而单独的Aβ42产生高达十二聚体的寡聚体。这表明Aβ40抑制Aβ42的寡聚化。