Human Anti-ADDL Recombinant Antibody (TAB-0813CLV) (CAT#: TAB-0813CLV)

Limbocker, Ryan, et al. "Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes." Nature communications 10.1 (2019): 225. https://doi.org/10.1038/s41467-018-07699-5

This research article investigates the effects of trodusquemine, an aminosterol compound, on amyloid-beta (Aβ42) aggregation and toxicity in Alzheimer's disease. The study reveals a fascinating dual mechanism where trodusquemine enhances the rate of Aβ42 aggregation by accelerating secondary nucleation processes, while simultaneously reducing the toxicity of oligomeric species. Using chemical kinetics, atomic force microscopy, and transmission electron microscopy, the researchers demonstrate that trodusquemine promotes the formation of shorter fibrils with larger cross-sectional dimensions. Despite accelerating aggregation, trodusquemine significantly reduces Aβ42 oligomer toxicity in neuroblastoma cells by decreasing oligomer binding to cell membranes, and improves health in a C. elegans model of Alzheimer's disease.
Creative Biolabs provided the human anti-ADDLs therapeutic antibody (clone 19.3, TAB-0813CLV) used in dot blot assays to characterize the structural properties of Aβ42 oligomers. This antibody was crucial for confirming that the oligomers used in the toxicity experiments matched those previously reported in the literature, enabling reliable assessment of how trodusquemine affects Aβ42 oligomer structure and membrane interactions. The specificity of this antibody helped establish the mechanistic basis for trodusquemine's protective effects, supporting the study's conclusion that reducing oligomer toxicity represents a promising therapeutic strategy against Alzheimer's disease.