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AD/PD 2022 | Comparing binding characteristics to Aβ of lecanemab, aducanumab & gantenerumab

A spectrum of aggregated amyloid β (Aβ) species, ranging from dimers, oligomers, protofibrils, and insoluble fibrillar Aβ, exist in a complex equilibrium in the Alzheimer’s disease brain. The most toxic forms of Aβ are the lower molecular weight species known as Aβ oligomers and protofibrils. Through decades of research in an attempt to develop treatment strategies, immunotherapy against Aβ has emerged as a promising treatment for Alzheimer’s disease. Lars Lannfelt, MD, PhD, Uppsala University, Uppsala, Sweden, discusses a study comparing the binding characteristics to Aβ of three antibodies, lecanemab, aducanumab, and gantenerumab, by three different methods: inhibition ELISA, immunodepletion and Surface Plasmon Resonance. The main difference observed between the antibodies was that lecanemab has its strongest binding to protofibrils, one of the most toxic forms of Aβ, while aducanumab and gantenerumab bind strongly to fibrils. Prof. Lannfelt highlights that in vitro studies such as the one discussed are essential to infer how the antibodies behave in clinical studies. This interview took place at the AD/PD™ 2022 Conference in Barcelona, Spain.


Prof. Lannfelt is a Co-Founder of BioArtic