Wie kleine Amyloid-β-Peptide zum großen Problem im Gehirn werden können

Abstract

The formation of amyloid-β oligomers plays a key role in the onset of Alzheimer’s disease. We investigated the aggregation of amyloid-β oligomers by mass spectrometry and ion mobility spectrometry, revealing those structural properties, which lead to the formation of mature fibrils. We can show that the arrangement of the first oligomers is crucial for the topology of the resulting species, leading to the formation of non-toxic aggregates or fibrils.

Epitope characterization of proteins and aptamers with mass spectrometry

“…Formation and inhibition of such aggregates can be followed by LILBID-MS (Figure 6(A) to (C)). 30,31 Monoclonal antibodies offer a possible approach for inhibiting this aggregation and clearing Aβ plaques by selectively binding to and promoting the removal of Aβ peptides from the brain. 32…”

“…Formation and inhibition of such aggregates can be followed by LILBID-MS (Figure 6(A) to (C)). 30,31 Monoclonal antibodies offer a possible approach for inhibiting this aggregation and clearing Aβ plaques by selectively binding to and promoting the removal of Aβ peptides from the brain. 32 Extensive research is focused on understanding the specific interactions between Aβ1-42 and antibodies, including their binding affinities, kinetics, and mechanisms of action.…”