Beta-Amyloid (20-42)

Aβ(20-42) contains the C-terminal hydrophobic portion of amyloid-beta ending at Ala42. The fragment retains the strongly aggregation-associated C-terminal sequence and can be used to investigate C-terminal contributions to amyloid assembly and peptide interactions.

• amyloid-beta aggregation research
• Alzheimer's disease research
• structure-function studies
• sequence-fragment controls

N-terminal truncation and fragment boundaries can substantially change solubility, metal binding and aggregation behavior. This exact sequence should therefore be treated as a distinct research reagent rather than substituted with full-length Aβ.

1. Alzheimer's beta-amyloid: insights into fibril formation and structure from Congo red binding