Amyloid Beta 1–40 (Aβ40) oligomers are soluble, metastable assemblies of the 40-amino-acid β-amyloid peptide and represent an important intermediate species in the amyloid aggregation pathway. While Aβ40 is less aggregation-prone than Aβ42, its oligomeric forms are increasingly recognized for their biological relevance and contribution to amyloid dynamics in Alzheimer’s disease (AD).

Aβ40 oligomers are generated through controlled in vitro assembly of monomeric Aβ40 under defined conditions, yielding low- to mid-order soluble aggregates. These oligomeric species are structurally distinct from monomers and mature fibrils and display unique biochemical and biophysical properties, including enhanced surface hydrophobicity and conformational flexibility.

Functionally, Aβ40 oligomers have been implicated in modulating amyloid nucleation, cross-seeding interactions with other amyloidogenic proteins, and synaptic signaling pathways. They serve as valuable tools for dissecting early aggregation events, oligomer-specific toxicity, and isoform-dependent differences in amyloid behavior.

TDA-1202-100-datasheet.pdf