Amyloid beta protein: Abeta40 inhibits Abeta42 oligomerization.
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.
Murray
Megan M
MM
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106-950, USA.
Bernstein
Summer L
SL
Nyugen
Vy
V
Condron
Margaret M
MM
Teplow
David B
DB
Bowers
Michael T
MT
D000682:Amyloid / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000633:toxicity; D010446:Peptide Fragments / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000633:toxicity; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis; D013329:Structure-Activity Relationship
D000682:Amyloid; D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42)